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Phosphoserine aminotransferase from bacillus circulans subsp. alkalophilus

Analyse Phosphoserine aminotransferase from bacillus circulans subsp. alkalophilus in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1BT4
Type
protein
Length
361 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Phosphoserine aminotransferase
EC
2.6.1.52
UniProt
Q59196
Ligands
PLP
Pockets
2 · best druggability 0.42

Structure

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

ChainMoleculeTypeResiduesSecondary structureUniProt
APhosphoserine aminotransferase (EC 2.6.1.52)protein36141% helix, 17% strandQ59196

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

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11370.420.7522empty
2540.300.7615empty

Modifications

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

Compared structures

  • 1BT4 · Phosphoserine aminotransferase from bacillus circulans subsp. alkalophilus · the same entry in another collection · chain A against A, TM-score 1.00
  • Q59196 · AlphaFold monomer V2.0 prediction for phosphoserine aminotransferase (Q59196) · a predicted model of the same protein · chain A against A, TM-score 1.00

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