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Crystal structure of TUM1 protein from saccharomyces cerevisiae

Analyse Crystal structure of TUM1 protein from saccharomyces cerevisiae in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3UTN
Type: protein
Length: 304 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Thiosulfate sulfurtransferase TUM1
EC: 2.8.1.1
UniProt: Q08686
Ligands: SO4
Pockets: 2 · best druggability 0.42

Structure

x-ray diffraction · 1 distinct chain · 36% helix, 13% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
X	Thiosulfate sulfurtransferase TUM1 (EC 2.8.1.1)	protein	304	36% helix, 13% strand	Q08686

Ligands and binding sites

SO4 · Sulfate ion · ion · chains X
DMS · Dimethyl sulfoxide · additive · 9 copies · chains X

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

Pockets

2 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	121	0.42	0.76	19	DMS
2	97	0.40	0.76	21	empty

Compared structures

3UTN · Crystal structure of Tum1 protein from Saccharomyces cerevisiae · the same entry in another collection · chain X against X, TM-score 1.00
Q08686 · AlphaFold monomer V2.0 prediction for thiosulfate sulfurtransferase TUM1 (Q08686) · a predicted model of the same protein · chain X against A, TM-score 0.98

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 Q08686
Elsewhere: RCSB PDB 3UTN · PDBe 3UTN · UniProt Q08686

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