MolNFT v1 · #156316 · protein

Crystal structure of methionine aminopeptidase from pyrococcus furiosus

6M00: “Crystal structure of methionine aminopeptidase from pyrococcus furiosus”. X-ray diffraction, 1 ligand (CO), 3 pockets (best druggability 0.62). MolNFT v1 #156316 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 6M00
Type: protein
Length: 294 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Methionine aminopeptidase
EC: 3.4.11.18
UniProt: P56218
Ligands: CO
Pockets: 3 · best druggability 0.62

Structure

x-ray diffraction · 1 distinct chain · 32% helix, 31% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Methionine aminopeptidase (EC 3.4.11.18)	protein	294	32% helix, 31% strand	P56218

Ligands and binding sites

CO · Cobalt (II) ion · metal · 2 copies · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	165	0.62	0.84	38	CO
2	72	0.32	0.74	17	empty
3	61	0.29	0.73	14	empty

Compared structures

6M00 · crystal structure of Methionine aminopeptidase from 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

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 P56218
Elsewhere: RCSB PDB 6M00 · PDBe 6M00 · UniProt P56218

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