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Structure of escherichia COLI glutathione synthetase at pH 6.0.

Analyse Structure of escherichia COLI glutathione synthetase at pH 6.0. in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2GLT
Type: protein
Length: 296 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Glutathione biosynthetic ligase
EC: 6.3.2.3
UniProt: P04425
Pockets: 3 · best druggability 0.56

Structure

x-ray diffraction · 1 distinct chain · 35% helix, 30% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Glutathione biosynthetic ligase (EC 6.3.2.3)	protein	296	35% helix, 30% strand	P04425

Pockets

3 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	246	0.56	0.78	46	empty
2	57	0.30	0.76	15	empty
3	51	0.26	0.74	15	empty

Compared structures

2GLT · Structure of escherichia COLI glutathione synthetase at pH 6.0. · the same entry in another collection · chain A against A, TM-score 1.00
P04425 · AlphaFold monomer V2.0 prediction for glutathione synthetase (P04425) · 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 P04425
Elsewhere: RCSB PDB 2GLT · PDBe 2GLT · UniProt P04425

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