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Zinc 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:

Bromine (Br) 21 atoms

Zinc Binding Sites:

The binding sites of Zinc 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 Zinc atom.
In total 2 binding sites of Zinc 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 Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in 5mj6

Go back to Zinc Binding Sites List in 5mj6
Zinc binding site 1 out of 2 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 Zinc with other atoms in the Zn 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:Zn1136

b:31.7
occ:1.00
 NE2 A:HIS468 2.0 30.4 1.0
OE1 A:GLU487 2.0 32.5 1.0
NE2 A:HIS464 2.1 26.9 1.0
O13 A:7O21137 2.1 35.8 1.0
CD A:GLU487 2.9 36.6 1.0
CD2 A:HIS468 3.0 27.1 1.0
P12 A:7O21137 3.0 35.9 1.0
CE1 A:HIS468 3.0 32.8 1.0
CD2 A:HIS464 3.0 30.7 1.0
O14 A:7O21137 3.0 41.0 1.0
CE1 A:HIS464 3.1 30.8 1.0
OE2 A:GLU487 3.1 38.5 1.0
CE2 A:TYR549 3.7 37.5 1.0
N11 A:7O21137 3.8 34.0 1.0
OH A:TYR549 3.9 34.1 1.0
ND1 A:HIS468 4.1 30.0 1.0
CG A:HIS468 4.1 25.0 1.0
ND1 A:HIS464 4.1 28.8 1.0
C1 A:7O21137 4.1 37.5 1.0
CG A:HIS464 4.1 33.5 1.0
CZ A:TYR549 4.2 42.2 1.0
C15 A:7O21137 4.3 38.3 1.0
CG A:GLU487 4.3 32.9 1.0
OE1 A:GLU431 4.3 37.5 1.0
CB A:ALA490 4.4 33.6 1.0
C16 A:7O21137 4.5 38.9 1.0
CA A:GLU487 4.6 40.4 1.0
CD2 A:TYR549 4.7 34.8 1.0
CB A:GLU487 4.7 38.8 1.0
OE2 A:GLU465 5.0 37.9 1.0
CD A:GLU431 5.0 45.3 1.0

Zinc binding site 2 out of 2 in 5mj6

Go back to Zinc Binding Sites List in 5mj6
Zinc binding site 2 out of 2 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 Zinc with other atoms in the Zn 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
B:Zn1126

b:36.3
occ:1.00
 OE1 B:GLU487 2.0 43.5 1.0
NE2 B:HIS464 2.1 41.3 1.0
NE2 B:HIS468 2.1 38.4 1.0
O13 B:7O21127 2.3 47.8 1.0
O14 B:7O21127 2.4 46.1 1.0
P12 B:7O21127 2.8 40.0 1.0
CD B:GLU487 2.9 46.0 1.0
CD2 B:HIS464 2.9 42.2 1.0
CD2 B:HIS468 3.0 37.8 1.0
OE2 B:GLU487 3.0 48.9 1.0
CE1 B:HIS468 3.2 45.5 1.0
CE1 B:HIS464 3.2 40.0 1.0
CE2 B:TYR549 3.7 45.2 1.0
N11 B:7O21127 3.9 43.6 1.0
C1 B:7O21127 4.1 51.0 1.0
CG B:HIS464 4.1 41.1 1.0
C15 B:7O21127 4.2 47.0 1.0
CG B:HIS468 4.2 40.8 1.0
OH B:TYR549 4.2 43.1 1.0
ND1 B:HIS464 4.2 41.1 1.0
ND1 B:HIS468 4.2 45.7 1.0
CB B:ALA490 4.3 41.5 1.0
CZ B:TYR549 4.3 46.7 1.0
CG B:GLU487 4.3 36.0 1.0
CD2 B:TYR549 4.5 39.4 1.0
C16 B:7O21127 4.6 45.8 1.0
OE1 B:GLU431 4.8 56.3 1.0
CA B:GLU487 4.8 37.4 1.0
CB B:GLU487 4.8 34.6 1.0
OE2 B:GLU465 4.9 53.3 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: Wed Dec 16 06:33:12 2020

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