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E. COLI methionine aminopeptidase monometalated with inhibitor YE6

Analyse E. COLI methionine aminopeptidase monometalated with inhibitor YE6 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2P99
Type: protein
Length: 261 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Methionine aminopeptidase
EC: 3.4.11.18
UniProt: P0AE18
Ligands: YE6, MN, NA
Pockets: 1 · best druggability 0.54

Structure

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

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Methionine aminopeptidase (EC 3.4.11.18)	protein	261	28% helix, 28% strand	P0AE18

Ligands and binding sites

YE6 · 5-(2-chlorophenyl)furan-2-carbohydrazide · ligand · chains A
MN · Manganese (II) ion · metal · chains A
NA · Sodium ion · metal · 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.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	145	0.54	0.81	25	YE6

Compared structures

2P99 · E. coli methionine aminopeptidase monometalated with inhibitor YE6 · the same entry in another collection · chain A against A, TM-score 1.00
P0AE18 · AlphaFold monomer V2.0 prediction for methionine aminopeptidase (P0AE18) · 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 P0AE18
Elsewhere: RCSB PDB 2P99 · PDBe 2P99 · UniProt P0AE18

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