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Human glutathione S-transferase P1-1 Y49F mutant

Analyse Human glutathione S-transferase P1-1 Y49F mutant in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 22GS
Type: protein
Length: 416 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Glutathione S-transferase P1-1
EC: 2.5.1.18
UniProt: P09211
Pockets: 4 · best druggability 0.73

Structure

x-ray diffraction · 1 distinct chain · 62% helix, 9% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Glutathione S-transferase P1-1 (EC 2.5.1.18)	protein	208	62% helix, 9% strand	P09211

Ligands and binding sites

MES · 2-(N-morpholino)-ethanesulfonic acid · additive · 3 copies · chains A, B

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

Pockets

4 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	725	0.73	0.79	92	empty
2	91	0.37	0.75	17	empty
3	79	0.35	0.75	17	empty
4	65	0.30	0.74	16	MES

Interfaces

1 interface between chains.

A–B · 1258 Å² buried · 16 hydrogen bonds · protein-protein

Compared structures

22GS · Human glutathione S-transferase P1-1 Y49F mutant · 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 P09211
Elsewhere: RCSB PDB 22GS · PDBe 22GS · UniProt P09211

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