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Crystal structure of glutamate 1-semialdehyde aminotransferase complexed with pyridoxamine-5'-phosphate from bacillus subtilis

Analyse Crystal structure of glutamate 1-semialdehyde aminotransferase complexed with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3BS8
Type: protein
Length: 430 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Glutamate-1-semialdehyde 2,1-aminomutase
EC: 5.4.3.8
UniProt: P30949
Ligands: PMP
Pockets: 2 · best druggability 0.71

Structure

x-ray diffraction · 1 distinct chain · 41% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Glutamate-1-semialdehyde 2,1-aminomutase (EC 5.4.3.8)	protein	430	41% helix, 17% strand	P30949

Ligands and binding sites

PMP · 4'-deoxy-4'-aminopyridoxal-5'-phosphate · ligand · chains A

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

Pockets

2 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	827	0.71	0.76	83	PMP
2	136	0.40	0.74	29	empty

Compared structures

3BS8 · Crystal structure of Glutamate 1-Semialdehyde Aminotransferase complexed with… · the same entry in another collection · chain A against A, TM-score 1.00
P30949 · AlphaFold monomer V2.0 prediction for glutamate-1-semialdehyde 2,1-aminomutase (P30949) · 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 P30949
Elsewhere: RCSB PDB 3BS8 · PDBe 3BS8 · UniProt P30949

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