Crystal structure of human methionine aminopeptidase-2 in complex; with an inhibitor (S)-3-hydroxy-2-oxo-1-(2-oxo-1,2,3,4-tetrahydro- quinolin-6-yl)-pyrrolidine-3-carboxylic acid 3-chloro-5-fluoro- benzylamide

Structure

x-ray diffraction · 1 distinct chain · 33% helix, 26% strand (DSSP).

Ligands and binding sites

• HZK · (3~{S})-~{N}-[(3-chloranyl-5-fluoranyl-phenyl)methyl]-3-oxidanyl-2-oxidanylidene-1-(2-oxidanylidene-3,4-dihydro-1~{H}-quinolin-6-yl)pyrrolidine-3-carboxamide · ligand · chains A
• MN · Manganese (II) ion · metal · 2 copies · chains A
• EDO · 1,2-ethanediol · additive · 3 copies · chains A
• DMS · Dimethyl sulfoxide · additive · chains A
• GOL · Glycerol · additive · chains A

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

Pockets

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

Compared structures

• 6QED · CRYSTAL STRUCTURE OF HUMAN METHIONINE AMINOPEPTIDASE-2 IN COMPLEX; WITH AN INHIBITOR… · the same entry in another collection · chain A against A, TM-score 1.00
• P50579 · AlphaFold monomer V2.0 prediction for methionine aminopeptidase 2 (P50579) · 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 P50579
• Elsewhere: RCSB PDB 6QED · PDBe 6QED · UniProt P50579