› 7pfs

X-ray diffraction
2.7Å resolution

Crystal structure of ERAP2 aminopeptidase in complex with phosphinic pseudotripeptide ((1R)-1-Amino-3-phenylpropyl){2-([1,1:3,1-terphenyl]-5-ylmethyl)-3-[((2S)-1-amino-1-oxo-3-phenylpropan-2-yl)-amino]-3-oxopropyl}phosphinic acid

Released:
DOI: 10.2210/pdb7pfs/pdb
PDB entry 7pfs coloured by chain, front view.
PDB entry 7pfs coloured by chain, side view.
PDB entry 7pfs coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Inhibitor-Dependent Usage of the S1' Specificity Pocket of ER Aminopeptidase 2.
Mpakali A, Georgiadis D, Stratikos E, Giastas P
ACS Med Chem Lett 13 218-224 (2022)
PMID: 35178178

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-180097 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (4 distinct):
Endoplasmic reticulum aminopeptidase 2 Chains: A, B
Molecule details ›
Chains: A, B
Length: 963 amino acids
Theoretical weight: 111.01 KDa
Source organism: Homo sapiens
Expression system: Trichoplusia ni
UniProt:
  • Canonical: Q6P179 (Residues: 1-960; Coverage: 100%)
Gene names: ERAP2, LRAP
Sequence domains:

Ligands and Environments

Carbohydrate polymer : NEW Components: NAG, BMA
Carbohydrate polymer
Carbohydrate polymer : NEW Components: NAG
Carbohydrate polymer
Carbohydrate polymer : NEW Components: NAG, BMA, MAN
Carbohydrate polymer
5 bound ligands:
Ligand NAG 8 x NAG
Ligand 7OO 2 x 7OO
Ligand EDO 3 x EDO
Ligand IMD 1 x IMD
Ligand ZN 2 x ZN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PETRA III, EMBL c/o DESY BEAMLINE P13 (MX1)
Spacegroup: P21
Unit cell:
a: 75.135Å b: 133.822Å c: 128.703Å
α: 90° β: 90.285° γ: 90°
R-values:
R R work R free
0.191 0.188 0.238
Expression system: Trichoplusia ni

Quick links

Citations

1 mention without citation

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