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Crystal structure of glutathione transferase homolog from neisseria gonorrhoeae, target efi-501841, with bound glutathione

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

PDB: 4HOJ
Type: protein
Length: 197 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Regf protein
UniProt: O33374
Ligands: GSH, CA
Pockets: 2 · best druggability 0.55

Structure

x-ray diffraction · 1 distinct chain · 55% helix, 9% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Regf protein	protein	197	55% helix, 9% strand	O33374

Ligands and binding sites

GSH · Glutathione · ligand · chains A
CA · Calcium ion · metal · 2 copies · chains A
ACT · Acetate ion · additive · chains A

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

Pockets

2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	146	0.55	0.81	25	ACT
2	185	0.54	0.79	27	GSH

Modifications

Observed in the structure: 1 covalent (covalent ligand).

Compared structures

4HOJ · Crystal structure of glutathione transferase homolog from Neisseria Gonorrhoeae, target… · 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 O33374
Elsewhere: RCSB PDB 4HOJ · PDBe 4HOJ · UniProt O33374

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