MolNFT v1 · #35734 · protein

Aminopeptidase from aneurinibacillus sp. strain am-1 with bestatin

2EK9: “Aminopeptidase from aneurinibacillus sp. strain am-1 with bestatin”. X-ray diffraction, 2 ligands (BES, ZN), 3 pockets (best druggability 0.53). MolNFT v1 #35734 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 2EK9
Type: protein
Length: 412 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Aminopeptidase
UniProt: A2V759
Ligands: BES, ZN
Pockets: 3 · best druggability 0.53

Structure

x-ray diffraction · 1 distinct chain · 31% helix, 27% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Aminopeptidase	protein	412	31% helix, 27% strand	A2V759

Ligands and binding sites

BES · 2-(3-amino-2-hydroxy-4-phenyl-butyrylamino)-4-methyl-pentanoic acid · ligand · chains A
ZN · Zinc ion · metal · 6 copies · chains A
IPA · Isopropyl alcohol · additive · 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	295	0.53	0.74	32	empty
2	99	0.47	0.81	21	ZN, BES
3	55	0.27	0.74	20	empty

Compared structures

2EK9 · Aminopeptidase from Aneurinibacillus sp. strain AM-1 with Bestatin · the same entry in another collection · 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 A2V759
Elsewhere: RCSB PDB 2EK9 · PDBe 2EK9 · UniProt A2V759

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