Research workbench

Apoenzyme structure of homoglutathione synthetase from glycine max in open conformation

Analyse Apoenzyme structure of homoglutathione synthetase from glycine max in open… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3KAJ
Type: protein
Length: 894 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Homoglutathione synthetase
EC: 6.3.2.3
UniProt: Q9M426
Pockets: 12 · best druggability 0.73

Structure

x-ray diffraction · 2 distinct chains · 41% helix, 26% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Homoglutathione synthetase (EC 6.3.2.3)	protein	452	40% helix, 27% strand	Q9M426
B	Homoglutathione synthetase (EC 6.3.2.3)	protein	442	42% helix, 26% strand	Q9M426

Pockets

12 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	847	0.73	0.77	94	empty
2	377	0.65	0.79	43	empty
3	524	0.62	0.75	51	empty
4	211	0.61	0.81	23	empty
5	251	0.57	0.78	20	empty

Interfaces

1 interface between chains.

A–B · 1225 Å² buried · 18 hydrogen bonds · protein-protein

Compared structures

3KAJ · Apoenzyme structure of homoglutathione synthetase from Glycine max in open conformation · 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 Q9M426
Elsewhere: RCSB PDB 3KAJ · PDBe 3KAJ · UniProt Q9M426

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