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Crystal structure of 26 kda GST of clonorchis sinensis in P3221 symmetry

Analyse Crystal structure of 26 kda GST of clonorchis sinensis in P3221 symmetry in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3ISO
Type: protein
Length: 436 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Putative glutathione transferase
UniProt: Q25595
Ligands: GSH, ZN, SO4
Pockets: 2 · best druggability 0.79

Structure

x-ray diffraction · 1 distinct chain · 55% helix, 8% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Putative glutathione transferase	protein	218	55% helix, 8% strand	Q25595

Ligands and binding sites

GSH · Glutathione · ligand · 2 copies · chains A, B
ZN · Zinc ion · metal · 2 copies · chains A, B
SO4 · Sulfate ion · ion · 8 copies · chains A, B

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	973	0.79	0.81	98	GSH
2	52	0.28	0.75	15	empty

Interfaces

1 interface between chains.

A–B · 1364 Å² buried · 17 hydrogen bonds · protein-protein

Compared structures

3ISO · Crystal structure of 26 kDa GST of Clonorchis sinensis in P3221 symmetry · the same entry in another collection · 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 Q25595
Elsewhere: RCSB PDB 3ISO · PDBe 3ISO · UniProt Q25595

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