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O-acetylserine sulfhydrylase from salmonella typhimurium

Analyse O-acetylserine sulfhydrylase from salmonella typhimurium in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1OAS
Type: protein
Length: 630 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: O-acetylserine sulfhydrylase
EC: 4.2.99.8
UniProt: P0A1E3
Ligands: PLP
Pockets: 4 · best druggability 0.78

Structure

x-ray diffraction · 1 distinct chain · 43% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	O-acetylserine sulfhydrylase (EC 4.2.99.8)	protein	315	43% helix, 17% strand	P0A1E3

Ligands and binding sites

PLP · Pyridoxal-5'-phosphate · ligand · 2 copies · chains A, B

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	1092	0.78	0.80	107	PLP
2	125	0.50	0.80	21	empty
3	51	0.30	0.76	11	empty
4	51	0.28	0.75	18	empty

Interfaces

1 interface between chains.

A–B · 2527 Å² buried · 32 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 cofactor (pyridoxal phosphate Schiff base).

Compared structures

1OAS · O-acetylserine sulfhydrylase from salmonella typhimurium · the same entry in another collection · chain A against A, TM-score 1.00
P0A1E3 · AlphaFold monomer V2.0 prediction for cysteine synthase a (P0A1E3) · 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 P0A1E3
Elsewhere: RCSB PDB 1OAS · PDBe 1OAS · UniProt P0A1E3

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