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

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: 4GCI
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, CL
Pockets: 3 · best druggability 0.78

Structure

x-ray diffraction · 1 distinct chain · 53% helix, 10% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Glutathione S-transferase	protein	202	53% helix, 10% strand	Q8D0L3

Ligands and binding sites

GSH · Glutathione · ligand · 2 copies · chains A, B
CL · Chloride ion · ion · 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	929	0.78	0.80	83	GSH
2	142	0.43	0.75	30	empty
3	123	0.43	0.76	27	empty

Interfaces

1 interface between chains.

A–B · 1614 Å² buried · 16 hydrogen bonds · protein-protein

Compared structures

4GCI · 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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Every structure of UniProt Q8D0L3
Elsewhere: RCSB PDB 4GCI · PDBe 4GCI · UniProt Q8D0L3

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