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Crystal structure of homoserine transacetylase

Analyse Crystal structure of homoserine transacetylase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2B61
Type: protein
Length: 357 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Homoserine O-acetyltransferase
EC: 2.3.1.31
UniProt: P45131
Pockets: 2 · best druggability 0.66

Structure

x-ray diffraction · 1 distinct chain · 38% helix, 18% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Homoserine O-acetyltransferase (EC 2.3.1.31)	protein	357	38% helix, 18% strand	P45131

Pockets

2 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	373	0.66	0.80	48	empty
2	55	0.27	0.73	14	empty

Modifications

Observed in the structure: 8 modified (engineered).

Compared structures

2B61 · Crystal Structure of Homoserine Transacetylase · the same entry in another collection · chain A against A, TM-score 1.00
P45131 · AlphaFold monomer V2.0 prediction for homoserine O-acetyltransferase (P45131) · 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 P45131
Elsewhere: RCSB PDB 2B61 · PDBe 2B61 · UniProt P45131

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