› 8khn

X-ray diffraction
1.51Å resolution

Crystal structure of human methionine aminopeptidase 12 (MAP12) in complex with two cobalt ions

Released:
DOI: 10.2210/pdb8khn/pdb
PDB entry 8khn coloured by chain, front view.
PDB entry 8khn coloured by chain, side view.
PDB entry 8khn coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural insights into N-terminal methionine cleavage by the human mitochondrial methionine aminopeptidase, MetAP1D.
Lee Y, Kim H, Lee E, Hahn H, Heo Y, Jang DM, Kwak K, Kim HJ, Kim HS
OpenAccess logo Sci Rep 13 22326 (2023)
PMID: 38102161

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-274921 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Methionine aminopeptidase 1D, mitochondrial Chain: A
Molecule details ›
Chain: A
Length: 313 amino acids
Theoretical weight: 34.38 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q6UB28 (Residues: 44-335; Coverage: 87%)
Gene names: MAP1D, METAP1D
Sequence domains: Metallopeptidase family M24

Ligands and Environments

2 bound ligands:
Ligand CO 2 x CO
Ligand PGE 1 x PGE
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PAL/PLS BEAMLINE 5C (4A)
Spacegroup: C2
Unit cell:
a: 78.916Å b: 80.978Å c: 49.033Å
α: 90° β: 102.21° γ: 90°
R-values:
R R work R free
0.194 0.193 0.214
Expression system: Escherichia coli BL21(DE3)

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