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Crystal structure of O-actetyl homoserine sulfhydrylase from thermus thermophilus HB8,OAH2.

Analyse Crystal structure of O-actetyl homoserine sulfhydrylase from thermus… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2CB1
Type: protein
Length: 404 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: O-acetyl homoserine sulfhydrylase
EC: 4.2.99.10
UniProt: Q76K51
Ligands: PLP
Pockets: 2 · best druggability 0.50

Structure

x-ray diffraction · 1 distinct chain · 43% helix, 14% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	O-acetyl homoserine sulfhydrylase (EC 4.2.99.10)	protein	404	43% helix, 14% strand	Q76K51

Ligands and binding sites

PLP · Pyridoxal-5'-phosphate · ligand · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

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	71	0.50	0.85	21	PLP
2	151	0.42	0.75	25	empty

Modifications

Observed in the structure: 1 cofactor (pyridoxal phosphate Schiff base).

Compared structures

2CB1 · Crystal Structure of O-actetyl Homoserine Sulfhydrylase From Thermus Thermophilus… · the same entry in another collection · chain A against A, TM-score 1.00

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Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt Q76K51
Elsewhere: RCSB PDB 2CB1 · PDBe 2CB1 · UniProt Q76K51

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