GL1X · GenesisL1 explorer

Research workbench

Crystal structure of histidinol-phosphate aminotransferase complexed with pyridoxal 5'-phosphate

Analyse Crystal structure of histidinol-phosphate 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
1GEW
Type
protein
Length
333 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Histidinol-phosphate aminotransferase
EC
2.6.1.9
UniProt
P06986
Ligands
PLP
Pockets
1 · best druggability 0.50

Structure

x-ray diffraction · 1 distinct chain · 41% helix, 16% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AHistidinol-phosphate aminotransferase (EC 2.6.1.9)protein33341% helix, 16% strandP06986

Ligands and binding sites

  • PLP · Pyridoxal-5'-phosphate · ligand · chains A

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

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11260.500.8027PLP

Modifications

Observed in the structure: 1 cofactor (pyridoxal phosphate Schiff base).

Compared structures

  • 1GEW · Crystal structure of histidinol-phosphate aminotransferase complexed with pyridoxal… · the same entry in another collection · chain A against A, TM-score 1.00
  • P06986 · AlphaFold monomer V2.0 prediction for histidinol-phosphate aminotransferase (P06986) · a predicted model of the same protein · chain A against A, TM-score 0.99

Analyse

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