› 5ab0

X-ray diffraction
2.5Å resolution

Crystal structure of aminopeptidase ERAP2 with ligand

Released:
DOI: 10.2210/pdb5ab0/pdb
PDB entry 5ab0 coloured by chain, front view.
PDB entry 5ab0 coloured by chain, side view.
PDB entry 5ab0 coloured by chain, top view.
Source organisms:
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:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-165430 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (5 distinct):
Endoplasmic reticulum aminopeptidase 2 Chains: A, C
Molecule details ›
Chains: A, C
Length: 967 amino acids
Theoretical weight: 111.56 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:
DG025 Chains: E, F
Molecule details ›
Chains: E, F
Length: 10 amino acids
Theoretical weight: 1.31 KDa
Source organism: synthetic construct
Expression system: Not provided

Ligands and Environments

Carbohydrate polymer : NEW Components: NAG
Carbohydrate polymer
Carbohydrate polymer : NEW Components: NAG, BMA
Carbohydrate polymer
Carbohydrate polymer : NEW Components: NAG, BMA
Carbohydrate polymer
4 bound ligands:
Ligand ZN 2 x ZN
Ligand NAG 10 x NAG
Ligand EDO 4 x EDO
Ligand MES 1 x MES
1 modified residue:
Ligand LYN 2 x LYN

Experiments and Validation Details

Entry percentile scores
X-ray source: ALBA BEAMLINE XALOC
Spacegroup: P21
Unit cell:
a: 75.35Å b: 134.42Å c: 129Å
α: 90° β: 90.49° γ: 90°
R-values:
R R work R free
0.201 0.198 0.258
Expression systems:
  • Trichoplusia ni
  • Not provided

Quick links

Citations

8 review citations

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

10 mentions without citation

Effects of Glycosylation on the Enzymatic Activity and Mechanisms of Proteases.
Goettig P. (2016)
9 more