› 2q8k

X-ray diffraction
1.6Å resolution

The crystal structure of Ebp1

Released:
DOI: 10.2210/pdb2q8k/pdb
PDB entry 2q8k coloured by chain, front view.
PDB entry 2q8k coloured by chain, side view.
PDB entry 2q8k coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
The crystal structure of Ebp1 reveals a methionine aminopeptidase fold as binding platform for multiple interactions.
Kowalinski E, Bange G, Bradatsch B, Hurt E, Wild K, Sinning I
FEBS Lett 581 4450-4 (2007)
PMID: 17765895

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-194061 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Proliferation-associated protein 2G4 Chain: A
Molecule details ›
Chain: A
Length: 401 amino acids
Theoretical weight: 44.74 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9UQ80 (Residues: 2-394; Coverage: 100%)
Gene names: EBP1, PA2G4
Sequence domains: Metallopeptidase family M24
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand SO4 5 x SO4
Ligand GOL 2 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-1
Spacegroup: P41212
Unit cell:
a: 73.887Å b: 73.887Å c: 183.348Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.184 0.182 0.219
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

10 review citations

The ERBB3 receptor in cancer and cancer gene therapy.
Sithanandam et al. (2008)
9 more

12 mentions without citation

A structural view of PA2G4 isoforms with opposing functions in cancer.
Stevenson et al. (2020)
11 more