› 2gu4

X-ray diffraction
1.8Å resolution

E. coli methionine aminopeptidase in complex with NleP, 1: 0.5, di-metalated

Released:
DOI: 10.2210/pdb2gu4/pdb
PDB entry 2gu4 coloured by chain, front view.
PDB entry 2gu4 coloured by chain, side view.
PDB entry 2gu4 coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Structural basis of catalysis by monometalated methionine aminopeptidase.
Ye QZ, Xie SX, Ma ZQ, Huang M, Hanzlik RP
Proc Natl Acad Sci U S A 103 9470-5 (2006)
PMID: 16769889

Function and Biology Details

Reaction catalysed: 
Release of N-terminal amino acids, preferentially methionine, from peptides and arylamides.
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-142397 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Methionine aminopeptidase Chains: A, B
Molecule details ›
Chains: A, B
Length: 263 amino acids
Theoretical weight: 29.21 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P0AE18 (Residues: 2-264; Coverage: 100%)
Gene names: JW0163, b0168, map
Sequence domains: Metallopeptidase family M24
Structure domains: Creatinase/methionine aminopeptidase superfamily

Ligands and Environments

3 bound ligands:
Ligand MN 4 x MN
Ligand NA 2 x NA
Ligand NLP 2 x NLP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: P21
Unit cell:
a: 49.704Å b: 64.034Å c: 76.347Å
α: 90° β: 108.1° γ: 90°
R-values:
R R work R free
0.206 0.195 0.227
Expression system: Escherichia coli BL21(DE3)

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Citations

3 review citations

Targeting Metalloenzymes for Therapeutic Intervention.
Chen et al. (2019)
2 more

1 mention without citation

Structural basis of catalysis by monometalated methionine aminopeptidase.
Ye et al. (2006)