Research workbench

Human 3-mercaptopyruvate sulfurtransferase

Analyse Human 3-mercaptopyruvate sulfurtransferase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3OLH
Type: protein
Length: 278 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: 3-mercaptopyruvate sulfurtransferase
EC: 2.8.1.2
UniProt: P25325
Ligands: NA, SO4
Pockets: 3 · best druggability 0.43

Structure

x-ray diffraction · 1 distinct chain · 33% helix, 12% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	3-mercaptopyruvate sulfurtransferase (EC 2.8.1.2)	protein	278	33% helix, 12% strand	P25325

Ligands and binding sites

NA · Sodium ion · metal · chains A
SO4 · Sulfate ion · ion · 2 copies · chains A

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

Pockets

3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	101	0.43	0.78	24	SO4
2	78	0.38	0.78	23	empty
3	53	0.33	0.78	18	empty

Compared structures

3OLH · Human 3-mercaptopyruvate sulfurtransferase · the same entry in another collection · chain A against A, TM-score 1.00
P25325 · AlphaFold monomer V2.0 prediction for 3-mercaptopyruvate sulfurtransferase (P25325) · 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 P25325
Elsewhere: RCSB PDB 3OLH · PDBe 3OLH · UniProt P25325

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