MolNFT v1 · #183006 · protein

Glutathione-S-transferase glig with partially disordered active site

7NC1 · Glutathione S-transferase glig: “Glutathione-S-transferase glig with partially disordered active site”. X-ray diffraction, 5 pockets (best druggability 0.67). MolNFT v1 #183006 on GenesisL1: 3D structure, binding sites and pockets…

PDB: 7NC1
Type: protein
Length: 419 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Glutathione S-transferase glig
UniProt: B0Y813
Pockets: 5 · best druggability 0.67

Structure

x-ray diffraction · 2 distinct chains · 44% helix, 10% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Glutathione S-transferase glig	protein	205	45% helix, 10% strand	B0Y813
B	Glutathione S-transferase glig	protein	214	44% helix, 11% strand	B0Y813

Ligands and binding sites

ACT · Acetate ion · additive · chains B

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

Pockets

5 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	264	0.67	0.83	26	empty
2	267	0.50	0.74	37	empty
3	131	0.37	0.73	19	empty
4	104	0.36	0.74	23	empty
5	55	0.27	0.73	15	empty

Interfaces

1 interface between chains.

A–B · 1452 Å² buried · 30 hydrogen bonds · protein-protein

Compared structures

7NC1 · Glutathione-S-transferase GliG with partially disordered active site · 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 B0Y813
Elsewhere: RCSB PDB 7NC1 · PDBe 7NC1 · UniProt B0Y813

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