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Crystal structure of type 1 human methionine aminopeptidase in complex with 3-(2,2-DIMETHYLPROPIONYLAMINO)PYRIDINE-2-carboxylic acid thiazole-2-ylamide

Analyse Crystal structure of type 1 human methionine aminopeptidase in complex with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2NQ7
Type
protein
Length
304 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Methionine aminopeptidase 1
EC
3.4.11.18
UniProt
P53582
Ligands
HM5, CO, K
Pockets
2 · best druggability 0.64

Structure

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

ChainMoleculeTypeResiduesSecondary structureUniProt
AMethionine aminopeptidase 1 (EC 3.4.11.18)protein30427% helix, 22% strandP53582

Ligands and binding sites

  • HM5 · 3-[(2,2-dimethylpropanoyl)amino]-N-1,3-thiazol-2-ylpyridine-2-carboxamide · ligand · chains A
  • CO · Cobalt (II) ion · metal · 3 copies · chains A
  • K · Potassium ion · metal · chains A
  • GOL · Glycerol · additive · 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, 2 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1500.640.9520GOL
22390.570.7835CO, HM5

Compared structures

  • 2NQ7 · Crystal structure of type 1 human methionine aminopeptidase in complex with… · 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

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