Bromine in PDB 3ejz: Structure of E203V Mutant E.Coli Cl-/H+ Exchanger, Clc-EC1
Protein crystallography data
The structure of Structure of E203V Mutant E.Coli Cl-/H+ Exchanger, Clc-EC1, PDB code: 3ejz
was solved by
H.-H.Lim,
C.Miller,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
58.76 /
2.90
|
Space group
|
C 1 2 1
|
Cell size a, b, c (Å), α, β, γ (°)
|
231.259,
96.415,
170.150,
90.00,
131.78,
90.00
|
R / Rfree (%)
|
25.2 /
28.1
|
Bromine Binding Sites:
The binding sites of Bromine atom in the Structure of E203V Mutant E.Coli Cl-/H+ Exchanger, Clc-EC1
(pdb code 3ejz). This binding sites where shown within
5.0 Angstroms radius around Bromine atom.
In total 4 binding sites of Bromine where determined in the
Structure of E203V Mutant E.Coli Cl-/H+ Exchanger, Clc-EC1, PDB code: 3ejz:
Jump to Bromine binding site number:
1;
2;
3;
4;
Bromine binding site 1 out
of 4 in 3ejz
Go back to
Bromine Binding Sites List in 3ejz
Bromine binding site 1 out
of 4 in the Structure of E203V Mutant E.Coli Cl-/H+ Exchanger, Clc-EC1
 Mono view
 Stereo pair view
|
A full contact list of Bromine with other atoms in the Br binding
site number 1 of Structure of E203V Mutant E.Coli Cl-/H+ Exchanger, Clc-EC1 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Br474
b:0.0
occ:1.00
|
OH
|
A:TYR445
|
1.7
|
0.7
|
1.0
|
CZ
|
A:TYR445
|
3.0
|
0.2
|
1.0
|
N
|
A:ILE356
|
3.2
|
82.3
|
1.0
|
CA
|
A:GLY355
|
3.2
|
0.3
|
1.0
|
OG
|
A:SER107
|
3.5
|
0.2
|
1.0
|
C
|
A:GLY355
|
3.7
|
100.0
|
1.0
|
CE2
|
A:TYR445
|
3.7
|
0.5
|
1.0
|
CB
|
A:SER107
|
3.7
|
0.5
|
1.0
|
N
|
A:PHE357
|
3.8
|
88.0
|
1.0
|
OE1
|
A:GLU148
|
3.9
|
88.6
|
1.0
|
N
|
A:GLY149
|
4.0
|
79.0
|
1.0
|
CE1
|
A:TYR445
|
4.1
|
0.7
|
1.0
|
CB
|
A:PHE357
|
4.1
|
88.0
|
1.0
|
CD1
|
A:ILE109
|
4.1
|
83.4
|
1.0
|
CA
|
A:GLY149
|
4.2
|
78.2
|
1.0
|
CA
|
A:ILE356
|
4.3
|
82.4
|
1.0
|
CG1
|
A:ILE109
|
4.4
|
83.1
|
1.0
|
CG2
|
A:ILE356
|
4.4
|
82.4
|
1.0
|
CA
|
A:SER107
|
4.4
|
0.4
|
1.0
|
N
|
A:GLY355
|
4.4
|
0.4
|
1.0
|
C
|
A:ILE356
|
4.5
|
82.5
|
1.0
|
CB
|
A:GLU148
|
4.5
|
85.5
|
1.0
|
CA
|
A:PHE357
|
4.5
|
87.9
|
1.0
|
CD1
|
A:PHE357
|
4.6
|
91.6
|
1.0
|
C
|
A:GLU148
|
4.8
|
85.5
|
1.0
|
CB
|
A:ILE356
|
4.8
|
82.3
|
1.0
|
CD
|
A:GLU148
|
4.8
|
89.9
|
1.0
|
CG
|
A:PHE357
|
4.8
|
89.8
|
1.0
|
O
|
A:GLY355
|
4.9
|
0.2
|
1.0
|
|
Bromine binding site 2 out
of 4 in 3ejz
Go back to
Bromine Binding Sites List in 3ejz
Bromine binding site 2 out
of 4 in the Structure of E203V Mutant E.Coli Cl-/H+ Exchanger, Clc-EC1
 Mono view
 Stereo pair view
|
A full contact list of Bromine with other atoms in the Br binding
site number 2 of Structure of E203V Mutant E.Coli Cl-/H+ Exchanger, Clc-EC1 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Br475
b:0.0
occ:1.00
|
N
|
A:SER107
|
2.9
|
0.6
|
1.0
|
CB
|
A:SER107
|
3.6
|
0.5
|
1.0
|
CA
|
A:GLY106
|
3.7
|
97.5
|
1.0
|
C
|
A:GLY106
|
3.8
|
96.9
|
1.0
|
CA
|
A:SER107
|
3.8
|
0.4
|
1.0
|
CZ
|
A:PHE348
|
3.8
|
83.8
|
1.0
|
CG2
|
A:ILE448
|
4.1
|
91.9
|
1.0
|
N
|
A:GLY108
|
4.1
|
0.3
|
1.0
|
CG
|
A:PRO110
|
4.1
|
96.3
|
1.0
|
CE1
|
A:PHE348
|
4.3
|
83.4
|
1.0
|
CD
|
A:PRO110
|
4.4
|
96.5
|
1.0
|
CD1
|
A:ILE448
|
4.4
|
92.2
|
1.0
|
C
|
A:SER107
|
4.5
|
0.2
|
1.0
|
OG
|
A:SER107
|
4.6
|
0.2
|
1.0
|
O
|
A:GLY105
|
4.7
|
0.5
|
1.0
|
CE2
|
A:PHE348
|
4.7
|
83.9
|
1.0
|
N
|
A:GLY106
|
4.9
|
98.7
|
1.0
|
O
|
A:GLY106
|
4.9
|
96.4
|
1.0
|
|
Bromine binding site 3 out
of 4 in 3ejz
Go back to
Bromine Binding Sites List in 3ejz
Bromine binding site 3 out
of 4 in the Structure of E203V Mutant E.Coli Cl-/H+ Exchanger, Clc-EC1
 Mono view
 Stereo pair view
|
A full contact list of Bromine with other atoms in the Br binding
site number 3 of Structure of E203V Mutant E.Coli Cl-/H+ Exchanger, Clc-EC1 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Br474
b:0.0
occ:1.00
|
OH
|
B:TYR445
|
1.4
|
0.6
|
1.0
|
CZ
|
B:TYR445
|
2.8
|
0.6
|
1.0
|
N
|
B:ILE356
|
3.2
|
73.6
|
1.0
|
CA
|
B:GLY355
|
3.4
|
82.0
|
1.0
|
OG
|
B:SER107
|
3.5
|
0.8
|
1.0
|
CE2
|
B:TYR445
|
3.5
|
0.5
|
1.0
|
N
|
B:PHE357
|
3.7
|
95.4
|
1.0
|
CB
|
B:SER107
|
3.7
|
0.7
|
1.0
|
C
|
B:GLY355
|
3.8
|
81.4
|
1.0
|
CE1
|
B:TYR445
|
3.8
|
0.7
|
1.0
|
OE1
|
B:GLU148
|
4.0
|
89.9
|
1.0
|
CB
|
B:PHE357
|
4.0
|
95.5
|
1.0
|
CG2
|
B:ILE356
|
4.2
|
72.3
|
1.0
|
CD1
|
B:ILE109
|
4.2
|
91.1
|
1.0
|
CA
|
B:ILE356
|
4.2
|
73.4
|
1.0
|
N
|
B:GLY149
|
4.3
|
98.1
|
1.0
|
C
|
B:ILE356
|
4.4
|
74.0
|
1.0
|
CA
|
B:PHE357
|
4.4
|
95.2
|
1.0
|
CD1
|
B:PHE357
|
4.4
|
99.2
|
1.0
|
CG1
|
B:ILE109
|
4.4
|
90.0
|
1.0
|
CA
|
B:GLY149
|
4.5
|
96.9
|
1.0
|
CA
|
B:SER107
|
4.5
|
0.5
|
1.0
|
N
|
B:GLY355
|
4.7
|
82.8
|
1.0
|
CB
|
B:ILE356
|
4.7
|
73.0
|
1.0
|
CB
|
B:GLU148
|
4.7
|
89.8
|
1.0
|
CG
|
B:PHE357
|
4.7
|
97.3
|
1.0
|
CD2
|
B:TYR445
|
4.9
|
0.0
|
1.0
|
CD
|
B:GLU148
|
4.9
|
91.0
|
1.0
|
|
Bromine binding site 4 out
of 4 in 3ejz
Go back to
Bromine Binding Sites List in 3ejz
Bromine binding site 4 out
of 4 in the Structure of E203V Mutant E.Coli Cl-/H+ Exchanger, Clc-EC1
 Mono view
 Stereo pair view
|
A full contact list of Bromine with other atoms in the Br binding
site number 4 of Structure of E203V Mutant E.Coli Cl-/H+ Exchanger, Clc-EC1 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Br475
b:0.0
occ:1.00
|
N
|
B:SER107
|
3.0
|
0.7
|
1.0
|
CB
|
B:SER107
|
3.6
|
0.7
|
1.0
|
CA
|
B:SER107
|
3.8
|
0.5
|
1.0
|
CZ
|
B:PHE348
|
3.9
|
78.8
|
1.0
|
C
|
B:GLY106
|
3.9
|
92.8
|
1.0
|
CG
|
B:PRO110
|
3.9
|
88.9
|
1.0
|
CG2
|
B:ILE448
|
3.9
|
95.4
|
1.0
|
CA
|
B:GLY106
|
3.9
|
93.4
|
1.0
|
N
|
B:GLY108
|
4.0
|
86.4
|
1.0
|
CD
|
B:PRO110
|
4.2
|
89.0
|
1.0
|
CD1
|
B:ILE448
|
4.3
|
95.0
|
1.0
|
CE1
|
B:PHE348
|
4.3
|
78.5
|
1.0
|
C
|
B:SER107
|
4.5
|
0.1
|
1.0
|
OG
|
B:SER107
|
4.5
|
0.8
|
1.0
|
CE2
|
B:PHE348
|
4.7
|
78.2
|
1.0
|
O
|
B:GLY105
|
4.8
|
91.3
|
1.0
|
CB
|
B:ILE448
|
5.0
|
95.7
|
1.0
|
|
Reference:
H.H.Lim,
C.Miller.
Intracellular Proton-Transfer Mutants in A Clc Cl-/H+ Exchanger. J.Gen.Physiol. V. 133 131 2009.
ISSN: ISSN 0022-1295
PubMed: 19139174
DOI: 10.1085/JGP.200810112
Page generated: Wed Jul 10 19:27:29 2024
|