MolNFT v1 · #2132 · protein

Human methionine aminopeptidase 2

1BN5: “Human methionine aminopeptidase 2”. X-ray diffraction, 1 ligand (CO), 4 pockets (best druggability 0.68). MolNFT v1 #2132 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 1BN5
Type: protein
Length: 355 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Methionine aminopeptidase
EC: 3.4.11.18
UniProt: P50579
Ligands: CO
Pockets: 4 · best druggability 0.68

Structure

x-ray diffraction · 1 distinct chain · 32% helix, 26% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Methionine aminopeptidase (EC 3.4.11.18)	protein	355	32% helix, 26% strand	P50579

Ligands and binding sites

CO · Cobalt (II) ion · metal · 2 copies · chains A
TBU · Tertiary-butyl alcohol · additive · 2 copies · 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, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	187	0.68	0.87	34	TBU
2	60	0.51	0.86	16	empty
3	52	0.29	0.76	12	empty
4	59	0.27	0.72	13	empty

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

1BN5 · Human methionine aminopeptidase 2 · 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 1BN5 · PDBe 1BN5 · UniProt P50579

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