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Methionine aminopeptidase from hyperthermophile pyrococcus furiosus

Analyse Methionine aminopeptidase from hyperthermophile pyrococcus furiosus in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1XGS
Type
protein
Length
590 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Methionine aminopeptidase
UniProt
P56218
Ligands
CO
Pockets
7 · best druggability 0.76

Structure

x-ray diffraction · 1 distinct chain · 32% helix, 28% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BMethionine aminopeptidaseprotein29532% helix, 28% strandP56218

Ligands and binding sites

  • CO · Cobalt (II) ion · metal · 4 copies · chains A, B

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1840.760.9824empty
23010.670.8249empty
31420.480.7819empty
41020.400.7624empty
5840.370.7616empty

Interfaces

1 interface between chains.

  • A–B · 1253 Ų buried · 16 hydrogen bonds · protein-protein

Compared structures

  • 1XGS · Methionine aminopeptidase from hyperthermophile pyrococcus furiosus · the same entry in another collection · chain A against A, TM-score 1.00
  • P56218 · AlphaFold monomer V2.0 prediction for methionine aminopeptidase (P56218) · a predicted model of the same protein · chain A against A, TM-score 0.99

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