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Crystal structure of multiple substrate aminotransferase (msat) from thermococcus profundus

Analyse Crystal structure of multiple substrate aminotransferase (msat) from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1WST
Type
protein
Length
403 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Multiple substrate aminotransferase
EC
2.6.1.-
UniProt
Q9V2W5
Ligands
PLP
Pockets
2 · best druggability 0.64

Structure

x-ray diffraction · 1 distinct chain · 48% helix, 15% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AMultiple substrate aminotransferase (EC 2.6.1.-)protein40348% helix, 15% strandQ9V2W5

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, 1 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
14430.640.7754PLP
2500.280.7517empty

Modifications

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

Compared structures

  • 1WST · Crystal structure of multiple substrate aminotransferase (MsAT) from Thermococcus… · the same entry in another collection · chain A against A, TM-score 1.00

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