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UniProt P00509

Aspartate aminotransferase (P00509)

Aspartate aminotransferase (UniProt P00509), EC 2.6.1.1: 178 experimental structures and 1 predicted model on GenesisL1, 4 ligands bound, 21 pockets. Binding sites, druggability and experiment against prediction (TM-score) in…

UniProt
P00509
Protein
Aspartate aminotransferase
EC
2.6.1.1
Experimental structures
178
Predicted models
1
Ligands
4
Pockets
21 · 2 records with a druggable one

Structures

179 records of P00509 in the MolNFT archive: 178 experimental, 1 predicted.

EntryTitleMethodChainsLigandsPockets
1AAMThe structural basis for the altered substrate specificity of the R292D active site mutant of…x-ray diffractionA——
1AAMThe structural basis for the altered substrate specificity of the R292D active site mutant of…x-ray diffractionA——
1AAWThe structural basis for the altered substrate specificity of the R292D active site mutant of…x-ray diffractionA——
1AAWThe structural basis for the altered substrate specificity of the R292D active site mutant of…x-ray diffractionA——
1AHEAspartate aminotransferase hexamutantx-ray diffractionA, B——
1AHEAspartate aminotransferase hexamutantx-ray diffractionA, B——
1AHFAspartate aminotransferase hexamutantx-ray diffractionA, B——
1AHFAspartate aminotransferase hexamutantx-ray diffractionA, B——
1AHGAspartate aminotransferase hexamutantx-ray diffractionA, B——
1AHGAspartate aminotransferase hexamutantx-ray diffractionA, B——
1AHXAspartate aminotransferase hexamutantx-ray diffractionA, B——
1AHXAspartate aminotransferase hexamutantx-ray diffractionA, B——
1AHYAspartate aminotransferase hexamutantx-ray diffractionA, B——
1AHYAspartate aminotransferase hexamutantx-ray diffractionA, B——
1AIAStructural basis for the catalytic activity of aspartate aminotransferase K258H lacking the…x-ray diffractionA, B——
1AIAStructural basis for the catalytic activity of aspartate aminotransferase K258H lacking the…x-ray diffractionA, B——
1AIBStructural basis for the catalytic activity of aspartate aminotransferase K258H lacking the…x-ray diffractionA, B——
1AIBStructural basis for the catalytic activity of aspartate aminotransferase K258H lacking the…x-ray diffractionA, B——
1AICStructural basis for the catalytic activity of aspartate aminotransferase K258H lacking the…x-ray diffractionA, B——
1AICStructural basis for the catalytic activity of aspartate aminotransferase K258H lacking the…x-ray diffractionA, B——
1AMQX-ray crystallographic study of pyridoxamine 5'-phosphate-type aspartate aminotransferases from…x-ray diffractionA——
1AMQX-ray crystallographic study of pyridoxamine 5'-phosphate-type aspartate aminotransferases from…x-ray diffractionA——
1AMRX-ray crystallographic study of pyridoxamine 5'-phosphate-type aspartate aminotransferases from…x-ray diffractionA——
1AMRX-ray crystallographic study of pyridoxamine 5'-phosphate-type aspartate aminotransferases from…x-ray diffractionA——
1AMSX-ray crystallographic study of pyridoxamine 5'-phosphate-type aspartate aminotransferases from…x-ray diffractionA——
1AMSX-ray crystallographic study of pyridoxamine 5'-phosphate-type aspartate aminotransferases from…x-ray diffractionA——
1ARGAspartate aminotransferase, phospho-5'-pyridoxyl aspartate complexx-ray diffractionA, B——
1ARGAspartate aminotransferase, phospho-5'-pyridoxyl aspartate complexx-ray diffractionA, B——
1ARHAspartate aminotransferase, Y225R/R386A mutantx-ray diffractionA, B——
1ARHAspartate aminotransferase, Y225R/R386A mutantx-ray diffractionA, B——
1ARIAspartate aminotransferase, W140H mutant, maleate complexx-ray diffractionA, B——
1ARIAspartate aminotransferase, W140H mutant, maleate complexx-ray diffractionA, B——
1ARSX-ray crystallographic study of pyridoxal 5'-phosphate-type aspartate aminotransferases from…x-ray diffractionA——
1ARSX-ray crystallographic study of pyridoxal 5'-phosphate-type aspartate aminotransferases from…x-ray diffractionA——
1ARTX-ray crystallographic study of pyridoxal 5'-phosphate-type aspartate aminotransferases from…x-ray diffractionA——
1ARTX-ray crystallographic study of pyridoxal 5'-phosphate-type aspartate aminotransferases from…x-ray diffractionA——
1ASAThe structural basis for the reduced activity of the Y226F(Y225F) active site mutant of E. COLI…x-ray diffractionA——
1ASAThe structural basis for the reduced activity of the Y226F(Y225F) active site mutant of E. COLI…x-ray diffractionA——
1ASBThe structural basis for the reduced activity of the D223A(D222A) active site mutant of E. COLI…x-ray diffractionA——
1ASBThe structural basis for the reduced activity of the D223A(D222A) active site mutant of E. COLI…x-ray diffractionA——
1ASCThe structural basis for the reduced activity of the D223A(D222A) active site mutant of E. COLI…x-ray diffractionA——
1ASCThe structural basis for the reduced activity of the D223A(D222A) active site mutant of E. COLI…x-ray diffractionA——
1ASDThe structure of wild type E. COLI aspartate aminotransferase reconstituted with N-meplpx-ray diffractionA——
1ASDThe structure of wild type E. COLI aspartate aminotransferase reconstituted with N-meplpx-ray diffractionA——
1ASEThe structure of wild type E. COLI aspartate aminotransferase reconstituted with plp-N-oxidex-ray diffractionA——
1ASEThe structure of wild type E. COLI aspartate aminotransferase reconstituted with plp-N-oxidex-ray diffractionA——
1ASFThe structural basis for the reduced activity of the Y226F(Y225F) active site mutant of E. COLI…x-ray diffractionA——
1ASFThe structural basis for the reduced activity of the Y226F(Y225F) active site mutant of E. COLI…x-ray diffractionA——
1ASGThe structural basis for the reduced activity of the Y226F(Y225F) active site mutant of E. COLI…x-ray diffractionA——
1ASGThe structural basis for the reduced activity of the Y226F(Y225F) active site mutant of E. COLI…x-ray diffractionA——
1ASLCrystal structures of escherichia COLI aspartate aminotransferase in two conformations: comparison…x-ray diffractionA, B——
1ASLCrystal structures of escherichia COLI aspartate aminotransferase in two conformations: comparison…x-ray diffractionA, B——
1ASMCrystal structures of escherichia COLI aspartate aminotransferase in two conformations: comparison…x-ray diffractionA, B——
1ASMCrystal structures of escherichia COLI aspartate aminotransferase in two conformations: comparison…x-ray diffractionA, B——
1ASNCrystal structures of escherichia COLI aspartate aminotransferase in two conformations: comparison…x-ray diffractionA, B——
1ASNCrystal structures of escherichia COLI aspartate aminotransferase in two conformations: comparison…x-ray diffractionA, B——
1B4XAspartate aminotransferase from E. COLI, C191S mutation, with bound maleatex-ray diffractionA——
1B4XAspartate aminotransferase from E. COLI, C191S mutation, with bound maleatex-ray diffractionA——
1BQAAspartate aminotransferase P195A mutantx-ray diffractionA, B——
1BQAAspartate aminotransferase P195A mutantx-ray diffractionA, B——

119 records more on the page itself.

Ligands

  • PLP · Pyridoxal-5'-phosphate · in 3 records
  • MAE · Maleic acid · in 2 records
  • PMP · 4'-deoxy-4'-aminopyridoxal-5'-phosphate · in 2 records
  • 77E · (4R)-4-amino-6-{3-hydroxy-2-methyl-5-[(phosphonooxy) methyl]pyridin-4-yl}hexanoic acid · in 1 record

Experiment against prediction

Elsewhere

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