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Crystal structure of glutahtione S-transferase homolog from yersinia pestis, target efi-501894, with bound glutathione

Analyse Crystal structure of glutahtione S-transferase homolog from yersinia pestis… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4G9H
Type: protein
Length: 404 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Glutathione S-transferase
UniProt: Q8D0L3
Ligands: GSH
Pockets: 3 · best druggability 0.78

Structure

x-ray diffraction · 1 distinct chain · 54% helix, 10% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Glutathione S-transferase	protein	202	54% helix, 10% strand	Q8D0L3

Ligands and binding sites

GSH · Glutathione · ligand · 2 copies · chains A, B
GOL · Glycerol · additive · 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, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	982	0.78	0.80	94	GSH
2	143	0.41	0.74	28	empty
3	124	0.41	0.75	29	GOL

Interfaces

1 interface between chains.

A–B · 1634 Å² buried · 17 hydrogen bonds · protein-protein

Compared structures

4G9H · Crystal structure of glutahtione s-transferase homolog from yersinia pestis, target… · the same entry in another collection · chain A against A, TM-score 1.00

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Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt Q8D0L3
Elsewhere: RCSB PDB 4G9H · PDBe 4G9H · UniProt Q8D0L3

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