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Bromine in PDB 5mj6: Ligand-Induced Conformational Change of Insulin-Regulated Aminopeptidase: Insights on Catalytic Mechanism and Active Site Plasticity.

Enzymatic activity of Ligand-Induced Conformational Change of Insulin-Regulated Aminopeptidase: Insights on Catalytic Mechanism and Active Site Plasticity.

All present enzymatic activity of Ligand-Induced Conformational Change of Insulin-Regulated Aminopeptidase: Insights on Catalytic Mechanism and Active Site Plasticity.:
3.4.11.3;

Protein crystallography data

The structure of Ligand-Induced Conformational Change of Insulin-Regulated Aminopeptidase: Insights on Catalytic Mechanism and Active Site Plasticity., PDB code: 5mj6 was solved by A.Mpakali, E.Stratikos, E.Saridakis, P.Giastas, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 40.81 / 2.53
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 112.240, 143.170, 148.990, 90.00, 90.00, 90.00
R / Rfree (%) 17.4 / 22.9

Other elements in 5mj6:

The structure of Ligand-Induced Conformational Change of Insulin-Regulated Aminopeptidase: Insights on Catalytic Mechanism and Active Site Plasticity. also contains other interesting chemical elements:

Zinc (Zn) 2 atoms

Bromine Binding Sites:

Pages:

>>> Page 1 <<< Page 2, Binding sites: 11 - 20; Page 3, Binding sites: 21 - 21;

Binding sites:

The binding sites of Bromine atom in the Ligand-Induced Conformational Change of Insulin-Regulated Aminopeptidase: Insights on Catalytic Mechanism and Active Site Plasticity. (pdb code 5mj6). This binding sites where shown within 5.0 Angstroms radius around Bromine atom.
In total 21 binding sites of Bromine where determined in the Ligand-Induced Conformational Change of Insulin-Regulated Aminopeptidase: Insights on Catalytic Mechanism and Active Site Plasticity., PDB code: 5mj6:
Jump to Bromine binding site number: 1; 2; 3; 4; 5; 6; 7; 8; 9; 10;

Bromine binding site 1 out of 21 in 5mj6

Go back to Bromine Binding Sites List in 5mj6
Bromine binding site 1 out of 21 in the Ligand-Induced Conformational Change of Insulin-Regulated Aminopeptidase: Insights on Catalytic Mechanism and Active Site Plasticity.


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 1 of Ligand-Induced Conformational Change of Insulin-Regulated Aminopeptidase: Insights on Catalytic Mechanism and Active Site Plasticity. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Br1138

b:71.9
occ:1.00
 CG2 A:THR561 3.4 58.0 1.0
CG1 A:VAL671 3.7 49.8 1.0
CB A:SER657 3.9 40.1 1.0
CG2 A:VAL671 3.9 55.1 1.0
CA A:TYR562 4.2 51.8 1.0
CB A:THR561 4.3 53.8 1.0
N A:TYR562 4.3 50.0 1.0
C A:THR561 4.3 56.9 1.0
O A:THR561 4.4 50.5 1.0
CD1 A:TYR562 4.5 53.8 1.0
CB A:VAL671 4.5 54.5 1.0
CB A:PRO655 4.5 50.0 1.0
CB A:TYR562 4.6 50.9 1.0
OG A:SER657 4.6 49.3 1.0
O A:PRO655 4.8 48.8 1.0
CA A:SER657 4.8 46.6 1.0
N A:SER657 4.9 57.5 1.0

Bromine binding site 2 out of 21 in 5mj6

Go back to Bromine Binding Sites List in 5mj6
Bromine binding site 2 out of 21 in the Ligand-Induced Conformational Change of Insulin-Regulated Aminopeptidase: Insights on Catalytic Mechanism and Active Site Plasticity.


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 2 of Ligand-Induced Conformational Change of Insulin-Regulated Aminopeptidase: Insights on Catalytic Mechanism and Active Site Plasticity. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Br1139

b:94.2
occ:1.00
 OD1 A:ASN834 3.4 76.8 1.0
SG A:CYS835 3.7 74.7 0.6
N A:ASN834 3.8 47.7 1.0
CA A:GLY833 3.8 47.8 1.0
CG A:GLN804 4.0 86.7 1.0
O A:HOH1341 4.2 66.6 1.0
C A:GLY833 4.3 51.3 1.0
CG2 A:ILE803 4.4 47.4 1.0
O A:HOH1331 4.4 50.5 1.0
CZ A:PHE796 4.5 48.4 1.0
CG A:ASN834 4.5 67.2 1.0
N A:CYS835 4.5 49.8 1.0
O5 A:NAG1130 4.6 96.9 1.0
CD A:GLN804 4.7 90.0 1.0
CA A:GLN804 4.7 58.7 1.0
C6 A:NAG1130 4.8 0.9 1.0
CE1 A:PHE796 4.8 52.9 1.0
N A:GLN804 4.8 56.5 1.0
CA A:ASN834 4.9 55.7 1.0
CB A:GLN804 4.9 66.7 1.0
N A:GLY833 4.9 58.5 1.0
O A:LEU832 5.0 51.3 1.0
C A:ASN834 5.0 58.4 1.0

Bromine binding site 3 out of 21 in 5mj6

Go back to Bromine Binding Sites List in 5mj6
Bromine binding site 3 out of 21 in the Ligand-Induced Conformational Change of Insulin-Regulated Aminopeptidase: Insights on Catalytic Mechanism and Active Site Plasticity.


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 3 of Ligand-Induced Conformational Change of Insulin-Regulated Aminopeptidase: Insights on Catalytic Mechanism and Active Site Plasticity. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Br1140

b:0.4
occ:1.00
 CD1 A:LEU557 4.0 42.3 1.0
CA A:PHE496 4.2 38.5 1.0
CD1 A:PHE496 4.2 51.9 1.0
NZ A:LYS560 4.3 60.1 1.0
O A:TYR495 4.3 39.7 1.0
N A:PHE496 4.4 45.0 1.0
C A:TYR495 4.5 45.5 1.0
CB A:PHE496 4.6 45.4 1.0
CE1 A:PHE492 4.8 45.4 1.0
CG A:PHE496 4.9 48.2 1.0
CE2 A:PHE511 5.0 46.7 1.0

Bromine binding site 4 out of 21 in 5mj6

Go back to Bromine Binding Sites List in 5mj6
Bromine binding site 4 out of 21 in the Ligand-Induced Conformational Change of Insulin-Regulated Aminopeptidase: Insights on Catalytic Mechanism and Active Site Plasticity.


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 4 of Ligand-Induced Conformational Change of Insulin-Regulated Aminopeptidase: Insights on Catalytic Mechanism and Active Site Plasticity. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Br1141

b:0.5
occ:1.00
 O A:SER180 3.9 40.6 1.0
OG A:SER180 4.1 59.1 1.0
O A:HOH1317 4.1 36.8 1.0
C A:SER180 4.1 42.6 1.0
C A:LEU181 4.3 47.0 1.0
CB A:SER180 4.3 42.7 1.0
N A:LEU181 4.3 44.8 1.0
N A:HIS182 4.3 40.0 1.0
CB A:HIS182 4.3 46.0 1.0
CA A:LEU181 4.5 39.9 1.0
O A:ARG191 4.6 47.4 1.0
CD1 A:ILE320 4.6 37.2 1.0
O A:LEU181 4.6 39.3 1.0
CA A:SER180 4.9 46.6 1.0
CA A:HIS182 4.9 40.8 1.0
CA A:GLY192 5.0 42.1 1.0
N A:SER193 5.0 40.1 1.0

Bromine binding site 5 out of 21 in 5mj6

Go back to Bromine Binding Sites List in 5mj6
Bromine binding site 5 out of 21 in the Ligand-Induced Conformational Change of Insulin-Regulated Aminopeptidase: Insights on Catalytic Mechanism and Active Site Plasticity.


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 5 of Ligand-Induced Conformational Change of Insulin-Regulated Aminopeptidase: Insights on Catalytic Mechanism and Active Site Plasticity. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Br1142

b:74.0
occ:1.00
 O B:HOH1274 3.3 35.5 1.0
NZ A:LYS911 3.5 66.3 1.0
O B:HOH1285 3.5 44.3 1.0
O B:GLY783 3.7 42.4 1.0
N B:MET785 3.7 37.7 1.0
N B:ASP786 3.8 47.4 1.0
N B:ALA1035 3.9 67.7 1.0
CE A:LYS911 4.0 65.3 1.0
CB B:ASP786 4.0 54.0 1.0
CB B:MET785 4.3 46.4 1.0
O B:ALA1035 4.4 84.3 1.0
C B:TYR784 4.4 40.1 1.0
CA B:MET785 4.4 47.6 1.0
CB B:ALA1035 4.5 50.3 1.0
CA B:TYR784 4.5 42.0 1.0
CA B:PRO1034 4.5 74.6 1.0
CD A:LYS911 4.6 57.7 1.0
CA B:ASP786 4.6 51.9 1.0
O B:HOH1206 4.6 55.2 1.0
CA B:ALA1035 4.6 62.0 1.0
C B:MET785 4.7 49.0 1.0
CG B:MET785 4.7 51.5 1.0
C B:PRO1034 4.7 69.2 1.0
C B:GLY783 4.8 49.5 1.0
CB B:PRO1034 4.9 65.3 1.0

Bromine binding site 6 out of 21 in 5mj6

Go back to Bromine Binding Sites List in 5mj6
Bromine binding site 6 out of 21 in the Ligand-Induced Conformational Change of Insulin-Regulated Aminopeptidase: Insights on Catalytic Mechanism and Active Site Plasticity.


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 6 of Ligand-Induced Conformational Change of Insulin-Regulated Aminopeptidase: Insights on Catalytic Mechanism and Active Site Plasticity. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Br1143

b:0.3
occ:1.00
 O A:HOH1350 3.1 39.9 1.0
CD2 A:TRP908 4.0 32.1 1.0
CE2 A:TRP908 4.0 35.2 1.0
CZ3 A:TRP874 4.3 41.7 1.0
NE1 A:TRP908 4.3 38.4 1.0
CG A:TRP908 4.3 35.5 1.0
CE3 A:TRP908 4.3 31.9 1.0
CZ2 A:TRP908 4.4 38.9 1.0
CB B:ALA1033 4.4 71.5 1.0
CH2 A:TRP874 4.5 47.2 1.0
CD1 A:TRP908 4.5 38.2 1.0
CZ3 A:TRP908 4.7 41.0 1.0
CH2 A:TRP908 4.7 31.8 1.0

Bromine binding site 7 out of 21 in 5mj6

Go back to Bromine Binding Sites List in 5mj6
Bromine binding site 7 out of 21 in the Ligand-Induced Conformational Change of Insulin-Regulated Aminopeptidase: Insights on Catalytic Mechanism and Active Site Plasticity.


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 7 of Ligand-Induced Conformational Change of Insulin-Regulated Aminopeptidase: Insights on Catalytic Mechanism and Active Site Plasticity. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Br1144

b:0.2
occ:1.00
 NZ A:LYS520 3.7 60.0 1.0
CD1 A:TRP1013 4.1 37.9 1.0
CD2 A:LEU774 4.1 53.1 1.0
CD1 A:LEU778 4.3 30.2 1.0
OD1 A:ASN1010 4.3 33.8 1.0
NE1 A:TRP1013 4.4 40.9 1.0
CG A:TRP1013 4.5 40.7 1.0
CG A:LEU774 4.7 42.1 1.0
CE A:LYS520 4.7 63.0 1.0
O A:HOH1252 4.7 37.6 1.0
CB A:TRP1013 4.9 38.7 1.0
CE2 A:TRP1013 5.0 35.1 1.0
CD2 A:TRP1013 5.0 38.5 1.0

Bromine binding site 8 out of 21 in 5mj6

Go back to Bromine Binding Sites List in 5mj6
Bromine binding site 8 out of 21 in the Ligand-Induced Conformational Change of Insulin-Regulated Aminopeptidase: Insights on Catalytic Mechanism and Active Site Plasticity.


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 8 of Ligand-Induced Conformational Change of Insulin-Regulated Aminopeptidase: Insights on Catalytic Mechanism and Active Site Plasticity. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Br1145

b:83.5
occ:1.00
 N A:ASP786 3.7 38.4 1.0
N A:MET785 3.8 35.5 1.0
O A:GLY783 3.8 51.3 1.0
N A:ALA1035 3.8 72.4 1.0
BR B:BR1101 3.9 0.6 1.0
CB A:ASP786 4.0 42.4 1.0
CA A:PRO1034 4.0 83.7 1.0
CB A:PRO1034 4.2 80.5 1.0
CB A:MET785 4.3 47.8 1.0
CA A:MET785 4.4 40.4 1.0
C A:TYR784 4.4 41.0 1.0
C A:PRO1034 4.4 76.0 1.0
CA A:ASP786 4.5 44.5 1.0
CA A:TYR784 4.6 42.7 1.0
C A:MET785 4.6 40.7 1.0
CG A:MET785 4.7 44.3 1.0
CB A:ALA1035 4.8 66.9 1.0
CE B:LYS911 4.8 71.4 1.0
CA A:ALA1035 4.9 75.0 1.0
C A:GLY783 4.9 50.8 1.0

Bromine binding site 9 out of 21 in 5mj6

Go back to Bromine Binding Sites List in 5mj6
Bromine binding site 9 out of 21 in the Ligand-Induced Conformational Change of Insulin-Regulated Aminopeptidase: Insights on Catalytic Mechanism and Active Site Plasticity.


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 9 of Ligand-Induced Conformational Change of Insulin-Regulated Aminopeptidase: Insights on Catalytic Mechanism and Active Site Plasticity. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Br1146

b:0.9
occ:1.00
 OE2 A:GLU285 3.9 79.2 0.5
OE1 A:GLU285 4.0 75.1 0.5
O6 A:MAN1117 4.0 86.7 1.0
CD A:GLU285 4.3 79.4 0.5
OG A:SER283 4.5 93.7 1.0
C6 A:MAN1117 4.5 84.9 1.0

Bromine binding site 10 out of 21 in 5mj6

Go back to Bromine Binding Sites List in 5mj6
Bromine binding site 10 out of 21 in the Ligand-Induced Conformational Change of Insulin-Regulated Aminopeptidase: Insights on Catalytic Mechanism and Active Site Plasticity.


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 10 of Ligand-Induced Conformational Change of Insulin-Regulated Aminopeptidase: Insights on Catalytic Mechanism and Active Site Plasticity. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Br1147

b:66.6
occ:1.00
 O A:HOH1323 3.5 32.8 1.0
CG1 A:ILE166 3.6 39.3 1.0
CD1 A:ILE166 3.6 50.5 1.0
NH1 A:ARG300 3.6 29.6 1.0
O A:HOH1236 4.0 47.8 1.0
O A:HIS240 4.2 43.5 1.0
CD1 A:LEU297 4.3 40.6 1.0
CB A:SER537 4.3 42.1 1.0
CD1 A:ILE540 4.4 41.7 1.0
NH2 A:ARG300 4.5 36.2 1.0
CZ A:ARG300 4.5 42.9 1.0
N A:SER537 4.6 40.8 1.0
CA A:SER537 4.6 42.5 1.0
O A:HOH1320 4.6 52.2 1.0
CD2 A:LEU297 4.8 35.0 1.0
CD2 A:HIS240 4.8 57.3 1.0
C A:HIS240 4.8 47.6 1.0

Reference:

A.Mpakali, E.Saridakis, K.Harlos, Y.Zhao, P.Kokkala, D.Georgiadis, P.Giastas, A.Papakyriakou, E.Stratikos. Ligand-Induced Conformational Change of Insulin-Regulated Aminopeptidase: Insights on Catalytic Mechanism and Active Site Plasticity. J. Med. Chem. V. 60 2963 2017.
ISSN: ISSN 1520-4804
PubMed: 28328206
DOI: 10.1021/ACS.JMEDCHEM.6B01890
Page generated: Thu Jul 11 00:19:17 2024

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