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Crystal structure of alanine-pyruvate aminotransferase with 2- methylserine

Analyse Crystal structure of alanine-pyruvate aminotransferase with 2- methylserine in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2YRI
Type
protein
Length
704 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Aminotransferase, class V
EC
2.6.-.-
UniProt
Q5SLX0
Ligands
MMM, PMP
Pockets
2 · best druggability 0.70

Structure

x-ray diffraction · 1 distinct chain · 44% helix, 16% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BAminotransferase, class V (EC 2.6.-.-)protein35244% helix, 16% strandQ5SLX0

Ligands and binding sites

  • MMM · (S,E)-3-hydroxy-2-((3-hydroxy-2-methyl-5-(phosphonooxymethyl)pyridin-4-yl)methyleneamino)-2-methylpropanoic acid · ligand · chains A, B
  • PMP · 4'-deoxy-4'-aminopyridoxal-5'-phosphate · ligand · chains A, B

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12890.700.8441PMP
22710.690.8442MMM

Interfaces

1 interface between chains.

  • A–B · 1980 Ų buried · 26 hydrogen bonds · protein-protein

Compared structures

  • 2YRI · Crystal structure of alanine-pyruvate aminotransferase with 2-methylserine · the same entry in another collection · chain A against A, TM-score 1.00

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