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Crystal structutre of thiobacillus thioparus THI115 carbonyl sulfide hydrolase / thiocyanate complex

Analyse Crystal structutre of thiobacillus thioparus THI115 carbonyl sulfide hydrolase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3VRK
Type: protein
Length: 212 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Carbonyl sulfide hydrolase
UniProt: H1AAP2
Ligands: ZN, NA, SCN
Pockets: 1 · best druggability 0.42

Structure

x-ray diffraction · 1 distinct chain · 34% helix, 14% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Carbonyl sulfide hydrolase	protein	212	34% helix, 14% strand	H1AAP2

Ligands and binding sites

ZN · Zinc ion · metal · chains A
NA · Sodium ion · metal · chains A
SCN · Thiocyanate ion · ion · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	132	0.42	0.75	25	SCN

Compared structures

3VRK · Crystal Structutre of Thiobacillus thioparus THI115 Carbonyl Sulfide Hydrolase /… · the same entry in another collection · chain A against A, TM-score 1.00
H1AAP2 · AlphaFold monomer V2.0 prediction for carbonyl sulfide hydrolase (H1AAP2) · a predicted model of the same protein · chain A against A, TM-score 0.96

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 H1AAP2
Elsewhere: RCSB PDB 3VRK · PDBe 3VRK · UniProt H1AAP2

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