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Crystal structure of truncated (delta 1-89) human methionine aminopeptidase type 1 in complex with N1-(5-chloro-6-methyl-2- (pyridin-2-YL)PYRIMIDIN-4-yl)-N2-(6-(TRIFLUOROMETHYL)PYRIDIN-2-yl) ethane-1,2-diamine

Analyse Crystal structure of truncated (delta 1-89) human methionine aminopeptidase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
4IKS
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
TFD, CO, K
Pockets
1 · best druggability 0.58

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

  • TFD · N-[5-chloro-6-methyl-2-(pyridin-2-yl)pyrimidin-4-yl]-N'-[6-(trifluoromethyl)pyridin-2-yl]ethane-1,2-diamine · 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

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12290.580.7934TFD, CO

Compared structures

  • 4IKS · Crystal structure of truncated (delta 1-89) human methionine aminopeptidase Type 1 in… · 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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