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URE2P5 from phanerochaete chrysosporium cocrystallized with 1-(S- glutathionyl)-2,4-dinitrobenzene.

Analyse URE2P5 from phanerochaete chrysosporium cocrystallized with 1-(S… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5O00
Type: protein
Length: 220 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Glutathione transferase URE2P5
UniProt: I7B368
Ligands: GDS, NIN, SO4
Pockets: 1 · best druggability 0.53

Structure

x-ray diffraction · 1 distinct chain · 59% helix, 9% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Glutathione transferase URE2P5	protein	220	59% helix, 9% strand	I7B368

Ligands and binding sites

GDS · Oxidized glutathione disulfide · ligand · chains A
NIN · Dinitrophenylene · ligand · chains A
SO4 · Sulfate ion · ion · 5 copies · chains A
GOL · Glycerol · additive · 5 copies · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	285	0.53	0.75	38	GDS, NIN

Compared structures

5O00 · Ure2p5 from Phanerochaete chrysosporium cocrystallized with… · 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 I7B368
Elsewhere: RCSB PDB 5O00 · PDBe 5O00 · UniProt I7B368

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