Human type 1 methionine aminopeptidase in complex with ovalicin at 1.1 ang

Structure

x-ray diffraction · 1 distinct chain · 27% helix, 22% strand (DSSP).

Ligands and binding sites

• OVA · 3,4-dihydroxy-2-methoxy-4-methyl-3-[2-methyl-3-(3-methyl-but-2-enyl) -oxiranyl]-cyclohexanone · ligand · chains A
• CO · Cobalt (II) ion · metal · 3 copies · chains A
• K · Potassium ion · metal · chains A
• GOL · Glycerol · additive · 2 copies · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Modifications

Observed in the structure: 1 covalent (covalent ligand).

Compared structures

• 2GZ5 · Human Type 1 methionine aminopeptidase in complex with ovalicin at 1.1 Ang · the same entry in another collection · chain A against A, TM-score 1.00
• P53582 · AlphaFold monomer V2.0 prediction for methionine aminopeptidase 1 (P53582) · a predicted model of the same protein · chain A against A, TM-score 1.00

Analyse

• Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
• Every structure of UniProt P53582
• Elsewhere: RCSB PDB 2GZ5 · PDBe 2GZ5 · UniProt P53582