› 4u70

X-ray diffraction
1.6Å resolution

HsMetAP (F309M) in complex with (1-amino-2-cyclohexylethyl)phosphonic acid

Released:
DOI: 10.2210/pdb4u70/pdb
PDB entry 4u70 coloured by chain, front view.
PDB entry 4u70 coloured by chain, side view.
PDB entry 4u70 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Identification of the molecular basis of inhibitor selectivity between the human and streptococcal type I methionine aminopeptidases.
Arya T, Reddi R, Kishor C, Ganji RJ, Bhukya S, Gumpena R, McGowan S, Drag M, Addlagatta A
J Med Chem 58 2350-7 (2015)
PMID: 25699713

Function and Biology Details

Reaction catalysed: 
Release of N-terminal amino acids, preferentially methionine, from peptides and arylamides.
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-156814 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Methionine aminopeptidase 1 Chain: A
Molecule details ›
Chain: A
Length: 306 amino acids
Theoretical weight: 34.44 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P53582 (Residues: 81-386; Coverage: 79%)
Gene names: KIAA0094, METAP1
Sequence domains: Metallopeptidase family M24
Structure domains: Creatinase/methionine aminopeptidase superfamily

Ligands and Environments

3 bound ligands:
Ligand CO 2 x CO
Ligand K 1 x K
Ligand Q04 1 x Q04
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007 HF
Spacegroup: P21
Unit cell:
a: 47.636Å b: 77.389Å c: 48.575Å
α: 90° β: 90.6° γ: 90°
R-values:
R R work R free
0.166 0.164 0.207
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Asymmetric Synthesis of Tetrasubstituted α-Aminophosphonic Acid Derivatives.
Maestro et al. (2021)
3 other articles