MolNFT v1 · #51644 · protein

Crystal structure of homoserine O-acetyltransferase (meta) from bacillus cereus with homoserine

2VDJ · Homoserine O-succinyltransferase: “Crystal structure of homoserine O-acetyltransferase (meta) from bacillus cereus with homoserine”. X-ray diffraction, 2 ligands (HSE, SO4), 1 pocket (best druggability 0.54). MolNFT v1 #51644 on…

PDB: 2VDJ
Type: protein
Length: 268 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Homoserine O-succinyltransferase
EC: 2.3.1.46
UniProt: Q72X44
Ligands: HSE, SO4
Pockets: 1 · best druggability 0.54

Structure

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

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Homoserine O-succinyltransferase (EC 2.3.1.46)	protein	268	32% helix, 28% strand	Q72X44

Ligands and binding sites

HSE · L-homoserine · ligand · chains A
SO4 · Sulfate ion · ion · 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	160	0.54	0.80	25	HSE

Compared structures

2VDJ · Crystal Structure of Homoserine O-acetyltransferase (metA) from Bacillus Cereus with… · the same entry in another collection · chain A against A, TM-score 1.00
Q72X44 · AlphaFold monomer V2.0 prediction for homoserine O-acetyltransferase (Q72X44) · a predicted model of the same protein · chain A against A, TM-score 0.93

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 Q72X44
Elsewhere: RCSB PDB 2VDJ · PDBe 2VDJ · UniProt Q72X44

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