MolNFT v1 · #109045 · protein

Thiosulfate dehydrogenase (tsda) from allochromatium vinosum - K208N mutant

4WQC: “Thiosulfate dehydrogenase (tsda) from allochromatium vinosum - K208N mutant”. X-ray diffraction, 3 ligands (HEC, THJ, SO4), 2 pockets (best druggability 0.72). MolNFT v1 #109045 on GenesisL1: 3D structure, binding sites and pockets…

PDB: 4WQC
Type: protein
Length: 229 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Thiosulfate dehydrogenase
EC: 1.8.2.2
UniProt: D3RVD4
Ligands: HEC, THJ, SO4
Pockets: 2 · best druggability 0.72

Structure

x-ray diffraction · 1 distinct chain · 39% helix, 6% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Thiosulfate dehydrogenase (EC 1.8.2.2)	protein	229	39% helix, 6% strand	D3RVD4

Ligands and binding sites

HEC · Heme C · ligand · 2 copies · chains A
THJ · Thiosulfate · ligand · chains A
SO4 · Sulfate ion · ion · chains A
EDO · 1,2-ethanediol · additive · 2 copies · 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, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	407	0.72	0.82	44	HEC, THJ
2	234	0.69	0.85	33	HEC

Modifications

Observed in the structure: 4 cofactor (heme c attachment).

Compared structures

D3RVD4 · AlphaFold monomer V2.0 prediction for thiosulfate dehydrogenase (D3RVD4) · 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 D3RVD4
Elsewhere: RCSB PDB 4WQC · PDBe 4WQC · UniProt D3RVD4

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