Bromine in PDB 2vr4: Transition-State Mimicry in Mannoside Hydrolysis: Characterisation of Twenty Six Inhibitors and Insight Into Binding From Linear Free Energy Relationships and 3-D Structure
Enzymatic activity of Transition-State Mimicry in Mannoside Hydrolysis: Characterisation of Twenty Six Inhibitors and Insight Into Binding From Linear Free Energy Relationships and 3-D Structure
All present enzymatic activity of Transition-State Mimicry in Mannoside Hydrolysis: Characterisation of Twenty Six Inhibitors and Insight Into Binding From Linear Free Energy Relationships and 3-D Structure:
3.2.1.25;
Protein crystallography data
The structure of Transition-State Mimicry in Mannoside Hydrolysis: Characterisation of Twenty Six Inhibitors and Insight Into Binding From Linear Free Energy Relationships and 3-D Structure, PDB code: 2vr4
was solved by
L.E.Tailford,
W.A.Offen,
N.L.Smith,
C.Dumon,
C.Moreland,
J.Gratien,
M.P.Heck,
R.V.Stick,
Y.Bleriot,
A.Vasella,
H.J.Gilbert,
G.J.Davies,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
65.37 /
1.8
|
Space group
|
P 1 21 1
|
Cell size a, b, c (Å), α, β, γ (°)
|
91.195,
114.738,
99.173,
90.00,
113.03,
90.00
|
R / Rfree (%)
|
17.7 /
22.2
|
Other elements in 2vr4:
The structure of Transition-State Mimicry in Mannoside Hydrolysis: Characterisation of Twenty Six Inhibitors and Insight Into Binding From Linear Free Energy Relationships and 3-D Structure also contains other interesting chemical elements:
Bromine Binding Sites:
The binding sites of Bromine atom in the Transition-State Mimicry in Mannoside Hydrolysis: Characterisation of Twenty Six Inhibitors and Insight Into Binding From Linear Free Energy Relationships and 3-D Structure
(pdb code 2vr4). This binding sites where shown within
5.0 Angstroms radius around Bromine atom.
In total 8 binding sites of Bromine where determined in the
Transition-State Mimicry in Mannoside Hydrolysis: Characterisation of Twenty Six Inhibitors and Insight Into Binding From Linear Free Energy Relationships and 3-D Structure, PDB code: 2vr4:
Jump to Bromine binding site number:
1;
2;
3;
4;
5;
6;
7;
8;
Bromine binding site 1 out
of 8 in 2vr4
Go back to
Bromine Binding Sites List in 2vr4
Bromine binding site 1 out
of 8 in the Transition-State Mimicry in Mannoside Hydrolysis: Characterisation of Twenty Six Inhibitors and Insight Into Binding From Linear Free Energy Relationships and 3-D Structure
Mono view
Stereo pair view
|
A full contact list of Bromine with other atoms in the Br binding
site number 1 of Transition-State Mimicry in Mannoside Hydrolysis: Characterisation of Twenty Six Inhibitors and Insight Into Binding From Linear Free Energy Relationships and 3-D Structure within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Br1877
b:23.2
occ:0.80
|
O
|
A:HOH2079
|
3.2
|
24.5
|
1.0
|
O
|
A:HOH2144
|
3.2
|
22.2
|
1.0
|
O
|
A:ILE107
|
3.5
|
24.3
|
1.0
|
N
|
A:ILE107
|
3.5
|
23.1
|
1.0
|
CB
|
A:LYS142
|
3.7
|
22.3
|
1.0
|
CB
|
A:PRO140
|
3.7
|
22.9
|
1.0
|
N
|
A:LYS142
|
3.8
|
20.9
|
1.0
|
CD1
|
A:ILE249
|
3.9
|
29.5
|
1.0
|
CA
|
A:GLY106
|
4.0
|
23.3
|
1.0
|
N
|
A:VAL141
|
4.0
|
21.8
|
1.0
|
CG1
|
A:ILE249
|
4.0
|
25.9
|
1.0
|
CA
|
A:PRO140
|
4.1
|
22.3
|
1.0
|
C
|
A:ILE107
|
4.2
|
24.5
|
1.0
|
C
|
A:PRO140
|
4.3
|
22.4
|
1.0
|
C
|
A:GLY106
|
4.3
|
23.7
|
1.0
|
CA
|
A:LYS142
|
4.4
|
22.7
|
1.0
|
CA
|
A:ILE107
|
4.5
|
23.3
|
1.0
|
OH
|
A:TYR218
|
4.8
|
22.6
|
1.0
|
CG
|
A:LYS142
|
4.9
|
22.8
|
1.0
|
O
|
A:ASP105
|
4.9
|
23.3
|
1.0
|
C
|
A:VAL141
|
4.9
|
19.4
|
1.0
|
CD
|
A:LYS142
|
5.0
|
24.2
|
1.0
|
|
Bromine binding site 2 out
of 8 in 2vr4
Go back to
Bromine Binding Sites List in 2vr4
Bromine binding site 2 out
of 8 in the Transition-State Mimicry in Mannoside Hydrolysis: Characterisation of Twenty Six Inhibitors and Insight Into Binding From Linear Free Energy Relationships and 3-D Structure
Mono view
Stereo pair view
|
A full contact list of Bromine with other atoms in the Br binding
site number 2 of Transition-State Mimicry in Mannoside Hydrolysis: Characterisation of Twenty Six Inhibitors and Insight Into Binding From Linear Free Energy Relationships and 3-D Structure within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Br1878
b:21.9
occ:0.90
|
N
|
A:HIS284
|
3.3
|
23.4
|
1.0
|
O
|
A:HOH2195
|
3.6
|
31.5
|
1.0
|
CA
|
A:ASN283
|
3.9
|
20.7
|
1.0
|
O
|
A:HIS284
|
4.0
|
25.4
|
1.0
|
C
|
A:ASN283
|
4.1
|
22.1
|
1.0
|
CA
|
A:HIS284
|
4.2
|
24.0
|
1.0
|
CB
|
A:HIS284
|
4.2
|
24.1
|
1.0
|
CD2
|
A:HIS284
|
4.3
|
28.1
|
1.0
|
O
|
A:ILE282
|
4.5
|
19.0
|
1.0
|
CB
|
A:ASN283
|
4.6
|
20.5
|
1.0
|
C
|
A:HIS284
|
4.6
|
24.4
|
1.0
|
CG
|
A:HIS284
|
4.7
|
26.2
|
1.0
|
OD1
|
A:ASN283
|
4.8
|
22.1
|
1.0
|
N
|
A:ASN283
|
4.9
|
19.0
|
1.0
|
|
Bromine binding site 3 out
of 8 in 2vr4
Go back to
Bromine Binding Sites List in 2vr4
Bromine binding site 3 out
of 8 in the Transition-State Mimicry in Mannoside Hydrolysis: Characterisation of Twenty Six Inhibitors and Insight Into Binding From Linear Free Energy Relationships and 3-D Structure
Mono view
Stereo pair view
|
A full contact list of Bromine with other atoms in the Br binding
site number 3 of Transition-State Mimicry in Mannoside Hydrolysis: Characterisation of Twenty Six Inhibitors and Insight Into Binding From Linear Free Energy Relationships and 3-D Structure within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Br1879
b:21.6
occ:0.60
|
O
|
A:HOH2561
|
3.2
|
15.7
|
1.0
|
O
|
A:HOH2341
|
3.4
|
37.4
|
1.0
|
CE2
|
A:TYR509
|
3.8
|
15.9
|
1.0
|
O
|
A:PHE492
|
4.0
|
16.9
|
1.0
|
CG
|
A:PRO497
|
4.0
|
15.1
|
1.0
|
CB
|
A:PRO497
|
4.1
|
14.5
|
1.0
|
CA
|
A:ARG493
|
4.1
|
18.4
|
1.0
|
CD2
|
A:TYR509
|
4.1
|
13.4
|
1.0
|
CB
|
A:HIS511
|
4.2
|
15.2
|
1.0
|
O
|
A:ARG493
|
4.5
|
18.4
|
1.0
|
CB
|
A:ARG493
|
4.6
|
18.6
|
1.0
|
N
|
A:HIS511
|
4.6
|
13.9
|
1.0
|
C
|
A:ARG493
|
4.7
|
18.3
|
1.0
|
CD2
|
A:HIS511
|
4.7
|
16.1
|
1.0
|
CG
|
A:ARG493
|
4.8
|
22.0
|
1.0
|
CG
|
A:HIS511
|
4.8
|
16.6
|
1.0
|
CA
|
A:HIS511
|
4.8
|
14.6
|
1.0
|
CD
|
A:PRO497
|
4.9
|
13.8
|
1.0
|
C
|
A:PHE492
|
4.9
|
17.7
|
1.0
|
|
Bromine binding site 4 out
of 8 in 2vr4
Go back to
Bromine Binding Sites List in 2vr4
Bromine binding site 4 out
of 8 in the Transition-State Mimicry in Mannoside Hydrolysis: Characterisation of Twenty Six Inhibitors and Insight Into Binding From Linear Free Energy Relationships and 3-D Structure
Mono view
Stereo pair view
|
A full contact list of Bromine with other atoms in the Br binding
site number 4 of Transition-State Mimicry in Mannoside Hydrolysis: Characterisation of Twenty Six Inhibitors and Insight Into Binding From Linear Free Energy Relationships and 3-D Structure within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Br1882
b:46.8
occ:0.50
|
O
|
A:HOH2258
|
2.8
|
25.9
|
1.0
|
O
|
A:ASN300
|
2.8
|
18.7
|
1.0
|
ND2
|
A:ASN390
|
2.9
|
14.6
|
1.0
|
O
|
A:HOH2259
|
3.1
|
25.7
|
1.0
|
CB
|
A:ASN390
|
3.7
|
13.1
|
1.0
|
CG
|
A:ASN390
|
3.8
|
13.9
|
1.0
|
O
|
A:HOH2279
|
3.9
|
28.4
|
1.0
|
C
|
A:ASN300
|
4.0
|
18.1
|
1.0
|
CA
|
A:GLY301
|
4.2
|
20.9
|
1.0
|
O
|
A:HOH2470
|
4.4
|
19.8
|
1.0
|
CD1
|
A:TRP302
|
4.4
|
21.3
|
1.0
|
NE1
|
A:TRP302
|
4.5
|
19.6
|
1.0
|
CE
|
A:LYS358
|
4.5
|
18.4
|
1.0
|
CG
|
A:MET355
|
4.6
|
13.0
|
1.0
|
N
|
A:GLY301
|
4.6
|
20.0
|
1.0
|
C
|
A:GLY301
|
4.6
|
22.2
|
1.0
|
SD
|
A:MET355
|
4.7
|
18.2
|
1.0
|
NZ
|
A:LYS358
|
4.7
|
17.8
|
1.0
|
N
|
A:TRP302
|
4.7
|
21.6
|
1.0
|
CG
|
A:TRP302
|
4.7
|
20.1
|
1.0
|
CE2
|
A:TRP302
|
4.8
|
20.2
|
1.0
|
O
|
A:PHE356
|
4.9
|
15.6
|
1.0
|
CD2
|
A:TRP302
|
5.0
|
18.6
|
1.0
|
|
Bromine binding site 5 out
of 8 in 2vr4
Go back to
Bromine Binding Sites List in 2vr4
Bromine binding site 5 out
of 8 in the Transition-State Mimicry in Mannoside Hydrolysis: Characterisation of Twenty Six Inhibitors and Insight Into Binding From Linear Free Energy Relationships and 3-D Structure
Mono view
Stereo pair view
|
A full contact list of Bromine with other atoms in the Br binding
site number 5 of Transition-State Mimicry in Mannoside Hydrolysis: Characterisation of Twenty Six Inhibitors and Insight Into Binding From Linear Free Energy Relationships and 3-D Structure within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Br1884
b:32.0
occ:0.70
|
N
|
A:ASP688
|
3.2
|
31.7
|
1.0
|
O
|
A:HOH2466
|
3.5
|
30.9
|
1.0
|
NE2
|
A:GLN685
|
3.6
|
25.8
|
1.0
|
CA
|
A:ASP688
|
3.7
|
32.2
|
1.0
|
N
|
A:ASN687
|
3.7
|
31.1
|
1.0
|
CG
|
A:GLN685
|
3.8
|
24.7
|
1.0
|
C
|
A:GLN686
|
3.9
|
29.2
|
1.0
|
CA
|
A:GLN686
|
4.0
|
28.7
|
1.0
|
CD
|
A:GLN685
|
4.2
|
26.0
|
1.0
|
C
|
A:ASN687
|
4.3
|
32.6
|
1.0
|
N
|
A:GLN686
|
4.3
|
26.6
|
1.0
|
O
|
A:GLN685
|
4.4
|
25.2
|
1.0
|
O
|
A:HOH2506
|
4.4
|
46.3
|
1.0
|
C
|
A:GLN685
|
4.4
|
26.2
|
1.0
|
CA
|
A:ASN687
|
4.5
|
32.3
|
1.0
|
O
|
A:GLN686
|
4.6
|
28.8
|
1.0
|
CB
|
A:ASP688
|
4.7
|
32.0
|
1.0
|
N
|
A:SER689
|
4.8
|
31.0
|
1.0
|
C
|
A:ASP688
|
4.8
|
31.7
|
1.0
|
CB
|
A:GLN685
|
5.0
|
25.2
|
1.0
|
|
Bromine binding site 6 out
of 8 in 2vr4
Go back to
Bromine Binding Sites List in 2vr4
Bromine binding site 6 out
of 8 in the Transition-State Mimicry in Mannoside Hydrolysis: Characterisation of Twenty Six Inhibitors and Insight Into Binding From Linear Free Energy Relationships and 3-D Structure
Mono view
Stereo pair view
|
A full contact list of Bromine with other atoms in the Br binding
site number 6 of Transition-State Mimicry in Mannoside Hydrolysis: Characterisation of Twenty Six Inhibitors and Insight Into Binding From Linear Free Energy Relationships and 3-D Structure within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Br1891
b:21.1
occ:0.50
|
O
|
A:HOH2167
|
3.2
|
29.7
|
1.0
|
O
|
A:HOH2144
|
3.2
|
22.2
|
1.0
|
NE2
|
A:GLN108
|
3.3
|
29.8
|
1.0
|
CG
|
A:GLN108
|
3.6
|
29.2
|
1.0
|
CB
|
A:PRO140
|
3.8
|
22.9
|
1.0
|
CD
|
A:PRO140
|
3.9
|
21.5
|
1.0
|
N
|
A:PRO140
|
3.9
|
21.4
|
1.0
|
ND2
|
A:ASN247
|
4.0
|
28.8
|
1.0
|
CD
|
A:GLN108
|
4.0
|
29.3
|
1.0
|
CA
|
A:PRO140
|
4.0
|
22.3
|
1.0
|
CG
|
A:PRO140
|
4.1
|
22.8
|
1.0
|
CG2
|
A:THR138
|
4.1
|
22.0
|
1.0
|
C
|
A:LEU139
|
4.4
|
21.8
|
1.0
|
O
|
A:HOH2145
|
4.5
|
19.8
|
1.0
|
OH
|
A:TYR218
|
4.7
|
22.6
|
1.0
|
O
|
A:LEU139
|
4.7
|
20.1
|
1.0
|
CB
|
A:GLN108
|
4.7
|
26.1
|
1.0
|
O
|
A:THR138
|
4.8
|
20.0
|
1.0
|
N
|
A:LEU139
|
4.9
|
20.9
|
1.0
|
C
|
A:THR138
|
4.9
|
21.2
|
1.0
|
CD1
|
A:ILE249
|
5.0
|
29.5
|
1.0
|
|
Bromine binding site 7 out
of 8 in 2vr4
Go back to
Bromine Binding Sites List in 2vr4
Bromine binding site 7 out
of 8 in the Transition-State Mimicry in Mannoside Hydrolysis: Characterisation of Twenty Six Inhibitors and Insight Into Binding From Linear Free Energy Relationships and 3-D Structure
Mono view
Stereo pair view
|
A full contact list of Bromine with other atoms in the Br binding
site number 7 of Transition-State Mimicry in Mannoside Hydrolysis: Characterisation of Twenty Six Inhibitors and Insight Into Binding From Linear Free Energy Relationships and 3-D Structure within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Br1884
b:30.8
occ:0.80
|
N
|
B:ASP688
|
3.3
|
29.1
|
1.0
|
NE2
|
B:GLN685
|
3.4
|
21.4
|
1.0
|
CA
|
B:ASP688
|
3.8
|
30.1
|
1.0
|
CG
|
B:GLN685
|
3.8
|
22.4
|
1.0
|
N
|
B:ASN687
|
3.9
|
27.5
|
1.0
|
C
|
B:GLN686
|
4.1
|
25.4
|
1.0
|
CD
|
B:GLN685
|
4.1
|
21.6
|
1.0
|
CA
|
B:GLN686
|
4.2
|
23.4
|
1.0
|
C
|
B:ASN687
|
4.3
|
29.6
|
1.0
|
O
|
B:HOH2471
|
4.4
|
33.6
|
1.0
|
O
|
B:GLN685
|
4.4
|
21.6
|
1.0
|
N
|
B:GLN686
|
4.4
|
22.1
|
1.0
|
C
|
B:GLN685
|
4.5
|
21.1
|
1.0
|
CA
|
B:ASN687
|
4.5
|
29.8
|
1.0
|
O
|
B:GLN686
|
4.7
|
24.7
|
1.0
|
CB
|
B:ASP688
|
4.8
|
31.6
|
1.0
|
CB
|
B:GLN685
|
4.9
|
20.7
|
1.0
|
C
|
B:ASP688
|
4.9
|
29.8
|
1.0
|
N
|
B:SER689
|
4.9
|
28.4
|
1.0
|
|
Bromine binding site 8 out
of 8 in 2vr4
Go back to
Bromine Binding Sites List in 2vr4
Bromine binding site 8 out
of 8 in the Transition-State Mimicry in Mannoside Hydrolysis: Characterisation of Twenty Six Inhibitors and Insight Into Binding From Linear Free Energy Relationships and 3-D Structure
Mono view
Stereo pair view
|
A full contact list of Bromine with other atoms in the Br binding
site number 8 of Transition-State Mimicry in Mannoside Hydrolysis: Characterisation of Twenty Six Inhibitors and Insight Into Binding From Linear Free Energy Relationships and 3-D Structure within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Br1885
b:22.7
occ:0.80
|
O
|
B:HOH2103
|
3.1
|
31.3
|
1.0
|
O
|
B:HOH2165
|
3.2
|
21.3
|
1.0
|
N
|
B:ILE107
|
3.5
|
19.0
|
1.0
|
O
|
B:ILE107
|
3.6
|
17.9
|
1.0
|
CB
|
B:LYS142
|
3.6
|
20.5
|
1.0
|
N
|
B:LYS142
|
3.8
|
19.0
|
1.0
|
CB
|
B:PRO140
|
3.9
|
20.3
|
1.0
|
CA
|
B:GLY106
|
4.0
|
18.9
|
1.0
|
CD1
|
B:ILE249
|
4.0
|
31.5
|
1.0
|
N
|
B:VAL141
|
4.1
|
18.4
|
1.0
|
CA
|
B:PRO140
|
4.1
|
19.2
|
1.0
|
CG1
|
B:ILE249
|
4.2
|
27.9
|
1.0
|
C
|
B:GLY106
|
4.3
|
17.7
|
1.0
|
C
|
B:ILE107
|
4.3
|
19.2
|
1.0
|
CA
|
B:LYS142
|
4.3
|
21.2
|
1.0
|
C
|
B:PRO140
|
4.4
|
19.3
|
1.0
|
CA
|
B:ILE107
|
4.5
|
18.2
|
1.0
|
O
|
B:ASP105
|
4.8
|
18.4
|
1.0
|
CG
|
B:LYS142
|
4.9
|
21.5
|
1.0
|
C
|
B:VAL141
|
4.9
|
18.2
|
1.0
|
CD
|
B:LYS142
|
4.9
|
20.1
|
1.0
|
|
Reference:
L.E.Tailford,
W.A.Offen,
N.L.Smith,
C.Dumon,
C.Morland,
J.Gratien,
M.P.Heck,
R.V.Stick,
Y.Bleriot,
A.Vasella,
H.J.Gilbert,
G.J.Davies.
Structural and Biochemical Evidence For A Boat-Like Transition State in Beta-Mannosidases. Nat.Chem.Biol. V. 4 306 2008.
ISSN: ISSN 1552-4450
PubMed: 18408714
DOI: 10.1038/NCHEMBIO.81
Page generated: Wed Jul 10 18:45:32 2024
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