› 2yd0

X-ray diffraction
2.7Å resolution

Crystal structure of the soluble domain of human endoplasmic reticulum aminopeptidase 1 ERAP1

Released:
DOI: 10.2210/pdb2yd0/pdb
PDB entry 2yd0 coloured by chain, front view.
PDB entry 2yd0 coloured by chain, side view.
PDB entry 2yd0 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Crystal structures of the endoplasmic reticulum aminopeptidase-1 (ERAP1) reveal the molecular basis for N-terminal peptide trimming.
Kochan G, Krojer T, Harvey D, Fischer R, Chen L, Vollmar M, von Delft F, Kavanagh KL, Brown MA, Bowness P, Wordsworth P, Kessler BM, Oppermann U
Proc Natl Acad Sci U S A 108 7745-50 (2011)
PMID: 21508329

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-192727 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
Endoplasmic reticulum aminopeptidase 1 Chain: A
Molecule details ›
Chain: A
Length: 897 amino acids
Theoretical weight: 102.6 KDa
Source organism: Homo sapiens
Expression system: Trichoplusia ni
UniProt:
  • Canonical: Q9NZ08 (Residues: 46-940; Coverage: 95%)
Gene names: APPILS, ARTS1, ERAP1, KIAA0525, UNQ584/PRO1154
Sequence domains:
Structure domains:

Ligands and Environments

Carbohydrate polymer : NEW Components: NAG
Carbohydrate polymer
5 bound ligands:
Ligand NAG 1 x NAG
Ligand ZN 1 x ZN
Ligand K 2 x K
Ligand EDO 1 x EDO
Ligand BES 1 x BES
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I03
Spacegroup: P622
Unit cell:
a: 200.948Å b: 200.948Å c: 114.222Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.155 0.152 0.215
Expression system: Trichoplusia ni

Quick links

Citations

55 review citations

Genetics of spondyloarthritis--beyond the MHC.
Reveille JD. (2012)
54 more

25 mentions without citation

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