Zinc in PDB 5c97: Insulin Regulated Aminopeptidase

All present enzymatic activity of Insulin Regulated Aminopeptidase:
3.4.11.3;

The structure of Insulin Regulated Aminopeptidase, PDB code: 5c97 was solved by A.Mpakali, E.Saridakis, K.Harlos, Y.Zhao, E.Stratikos, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	68.20 / 3.37
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	69.000, 260.151, 73.360, 90.00, 111.61, 90.00
R / Rfree (%)	21.6 / 28.5

The binding sites of Zinc atom in the Insulin Regulated Aminopeptidase (pdb code 5c97). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Insulin Regulated Aminopeptidase, PDB code: 5c97:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Insulin Regulated Aminopeptidase


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Insulin Regulated Aminopeptidase within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn1101 b:83.8 occ:0.72 OE1 A:GLU487 2.0 99.0 1.0 NE2 A:HIS464 2.0 94.9 1.0 NE2 A:HIS468 2.1 0.8 1.0 OE2 A:GLU487 2.5 0.4 1.0 CD A:GLU487 2.6 0.1 1.0 CD2 A:HIS468 2.6 0.1 1.0 CD2 A:HIS464 2.9 99.7 1.0 CE1 A:HIS464 2.9 91.2 1.0 CE1 A:HIS468 3.3 1.0 1.0 OE2 A:GLU431 3.8 0.1 1.0 CG A:HIS468 3.9 0.6 1.0 ND1 A:HIS464 4.0 93.8 1.0 CG A:HIS464 4.0 0.2 1.0 CG A:GLU487 4.1 98.1 1.0 ND1 A:HIS468 4.1 0.9 1.0 CG A:GLU431 4.3 1.0 1.0 CD A:GLU431 4.4 0.5 1.0 OE1 A:GLU465 4.5 0.9 1.0 OE2 A:GLU465 4.5 0.5 1.0 CD A:GLU465 4.7 0.8 1.0 CB A:GLU487 4.7 94.0 1.0 CB A:ALA490 4.8 88.1 1.0 CA A:GLU487 4.8 95.6 1.0

Zinc binding site 2 out of 2 in the Insulin Regulated Aminopeptidase


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Insulin Regulated Aminopeptidase within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn1101 b:0.5 occ:1.00 CE1 B:HIS468 1.9 0.1 1.0 OE1 B:GLU487 2.1 0.0 1.0 NE2 B:HIS464 2.1 0.4 1.0 OE2 B:GLU487 2.3 0.1 1.0 CD B:GLU487 2.5 0.7 1.0 NE2 B:HIS468 2.6 0.3 1.0 CD2 B:HIS464 2.7 0.6 1.0 ND1 B:HIS468 3.1 0.5 1.0 OE2 B:GLU431 3.3 0.9 1.0 CE1 B:HIS464 3.4 0.6 1.0 OE1 B:GLU465 3.5 0.3 1.0 OE2 B:GLU465 3.6 0.9 1.0 CD2 B:HIS468 3.9 0.2 1.0 CD B:GLU465 3.9 0.8 1.0 CG B:HIS464 4.0 0.5 1.0 CG B:GLU487 4.0 0.2 1.0 CG B:HIS468 4.1 0.2 1.0 CD B:GLU431 4.1 0.2 1.0 ND1 B:HIS464 4.3 0.3 1.0 OE1 B:GLU431 4.6 0.4 1.0 CB B:GLU487 4.8 0.2 1.0 CB B:ALA490 5.0 0.4 1.0

A.Mpakali, E.Saridakis, K.Harlos, Y.Zhao, A.Papakyriakou, P.Kokkala, D.Georgiadis, E.Stratikos. Crystal Structure of Insulin-Regulated Aminopeptidase with Bound Substrate Analogue Provides Insight on Antigenic Epitope Precursor Recognition and Processing. J Immunol. V. 195 2842 2015.
ISSN: ESSN 1550-6606
PubMed: 26259583
DOI: 10.4049/JIMMUNOL.1501103