› 5cu5

X-ray diffraction
3.02Å resolution

Crystal structure of ERAP2 without catalytic Zn(II) atom

Released:
DOI: 10.2210/pdb5cu5/pdb
PDB entry 5cu5 coloured by chain, front view.
PDB entry 5cu5 coloured by chain, side view.
PDB entry 5cu5 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural Basis for Antigenic Peptide Recognition and Processing by Endoplasmic Reticulum (ER) Aminopeptidase 2.
Mpakali A, Giastas P, Mathioudakis N, Mavridis IM, Saridakis E, Stratikos E
J Biol Chem 290 26021-32 (2015)
PMID: 26381406

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-180096 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (4 distinct):
Endoplasmic reticulum aminopeptidase 2 Chains: A, B
Molecule details ›
Chains: A, B
Length: 967 amino acids
Theoretical weight: 111.53 KDa
Source organism: Homo sapiens
Expression system: Trichoplusia ni
UniProt:
  • Canonical: Q6P179 (Residues: 1-960; Coverage: 100%)
Gene names: ERAP2, LRAP
Sequence domains:
Structure domains:

Ligands and Environments

Carbohydrate polymer : NEW Components: NAG, MAN
Carbohydrate polymer
Carbohydrate polymer : NEW Components: NAG
Carbohydrate polymer
Carbohydrate polymer : NEW Components: NAG, MAN
Carbohydrate polymer
1 bound ligand:
Ligand NAG 9 x NAG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06DA
Spacegroup: P21
Unit cell:
a: 74.65Å b: 135.17Å c: 126.49Å
α: 90° β: 90.74° γ: 90°
R-values:
R R work R free
0.213 0.21 0.263
Expression system: Trichoplusia ni

Quick links

Citations

9 review citations

How ERAP1 and ERAP2 Shape the Peptidomes of Disease-Associated MHC-I Proteins.
López de Castro JA. (2018)
8 more

6 mentions without citation

M1 aminopeptidases as drug targets: broad applications or therapeutic niche?
Drinkwater et al. (2017)
5 more