Research workbench

Glutathione-inhibited scgcl

Analyse Glutathione-inhibited scgcl in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3LVW
Type: protein
Length: 672 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Glutamate--cysteine ligase
EC: 6.3.2.2
UniProt: P32477
Ligands: GSH
Pockets: 6 · best druggability 0.72

Structure

x-ray diffraction · 1 distinct chain · 40% helix, 13% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Glutamate--cysteine ligase (EC 6.3.2.2)	protein	672	40% helix, 13% strand	P32477

Ligands and binding sites

GSH · Glutathione · ligand · chains A
PGE · Triethylene glycol · additive · 3 copies · chains A

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

Pockets

6 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	700	0.72	0.79	55	GSH, PGE
2	142	0.58	0.83	25	empty
3	355	0.57	0.75	41	empty
4	164	0.47	0.76	32	PGE
5	75	0.41	0.79	17	empty

Compared structures

3LVW · Glutathione-inhibited ScGCL · the same entry in another collection · chain A against A, TM-score 1.00
P32477 · AlphaFold monomer V2.0 prediction for glutamate--cysteine ligase (P32477) · a predicted model of the same protein · chain A against A, TM-score 0.99

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 P32477
Elsewhere: RCSB PDB 3LVW · PDBe 3LVW · UniProt P32477

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.