› 6m8p

X-ray diffraction
3.31Å resolution

Human ERAP1 bound to phosphinic pseudotripeptide inhibitor DG013

Released:
DOI: 10.2210/pdb6m8p/pdb
PDB entry 6m8p coloured by chain, front view.
PDB entry 6m8p coloured by chain, side view.
PDB entry 6m8p coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Conformational dynamics linked to domain closure and substrate binding explain the ERAP1 allosteric regulation mechanism.
Maben Z, Arya R, Georgiadis D, Stratikos E, Stern LJ
Nat Commun 12 5302 (2021)
PMID: 34489420

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
  • not assigned
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 Chains: A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q, R, S, T, U, V
Molecule details ›
Chains: A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q, R, S, T, U, V
Length: 899 amino acids
Theoretical weight: 102.97 KDa
Source organism: Homo sapiens
Expression system: Trichoplusia ni
UniProt:
  • Canonical: Q9NZ08 (Residues: 33-41, 42-43, 44-485, 514-940; Coverage: 94%)
Gene names: APPILS, ARTS1, ERAP1, KIAA0525, UNQ584/PRO1154
Sequence domains:

Ligands and Environments

Carbohydrate polymer : NEW Components: NAG, BMA
Carbohydrate polymer
4 bound ligands:
Ligand ZN 22 x ZN
Ligand P52 22 x P52
Ligand SO4 309 x SO4
Ligand NAG 22 x NAG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS-II BEAMLINE 17-ID-2
Unit cell:
a: 125.79Å b: 548.684Å c: 589.056Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.286 0.285 0.295
Expression system: Trichoplusia ni

Quick links

Citations

2 review citations

Mechanistic diversity in MHC class I antigen recognition.
Barbosa et al. (2021)
1 more

3 mentions without citation

Phosphinic Peptides as Tool Compounds for the Study of Pharmacologically Relevant Zn-Metalloproteases.
Georgiadis et al. (2022)
2 more