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UniProt P11961

P11961

P11961 (UniProt P11961): 33 experimental structures on GenesisL1. Binding sites, pockets, druggability and 3D structures in GL1X.

UniProt
P11961
Experimental structures
33
Predicted models
0

Structures

33 records of P11961 in the MolNFT archive: 33 experimental, 0 predicted.

EntryTitleMethodChainsLigandsPockets
1B5SDihydrolipoyl transacetylase (E.C.2.3.1.12) catalytic domain (residues 184-425) from bacillus…x-ray diffractionA, B, C, D, E——
1B5SDihydrolipoyl transacetylase (E.C.2.3.1.12) catalytic domain (residues 184-425) from bacillus…x-ray diffractionA, B, C, D, E——
1EBDDihydrolipoamide dehydrogenase complexed with the binding domain of the dihydrolipoamide acetylasex-ray diffractionC——
1EBDDihydrolipoamide dehydrogenase complexed with the binding domain of the dihydrolipoamide acetylasex-ray diffractionC——
1LABThree-dimensional structure of the lipoyl domain from bacillus stearothermophilus pyruvate…solution nmrA——
1LABThree-dimensional structure of the lipoyl domain from bacillus stearothermophilus pyruvate…solution nmrA——
1LACThree-dimensional structure of the lipoyl domain from bacillus stearothermophilus pyruvate…solution nmrA——
1LACThree-dimensional structure of the lipoyl domain from bacillus stearothermophilus pyruvate…solution nmrA——
1W3DNMR structure of the peripheral-subunit binding domain of Bacillus stearothermophilus E2psolution nmrA——
1W3DNMR structure of the peripheral-subunit binding domain of bacillus stearothermophilus E2Psolution nmrA——
1W4EPeripheral-subunit binding domains from mesophilic, thermophilic, and hyperthermophilic bacteria…solution nmrA——
1W4EPeripheral-subunit binding domains from mesophilic, thermophilic, and hyperthermophilic bacteria…solution nmrA——
1W4FPeripheral-subunit from mesophilic, thermophilic and hyperthermophilic bacteria fold by ultrafast…solution nmrA——
1W4FPeripheral-subunit from mesophilic, thermophilic and hyperthermophilic bacteria fold by ultrafast…solution nmrA——
1W4GPeripheral-subunit binding domains from mesophilic, thermophilic, and hyperthermophilic bacteria…solution nmrA——
1W4GPeripheral-subunit binding domains from mesophilic, thermophilic, and hyperthermophilic bacteria…solution nmrA——
1W4HPeripheral-subunit from mesophilic, thermophilic and hyperthermophilic bacteria fold by ultrafast…solution nmrA——
1W4HPeripheral-subunit from mesophilic, thermophilic and hyperthermophilic bacteria fold by ultrafast…solution nmrA——
1W85The crystal structure of pyruvate dehydrogenase E1 bound to the peripheral subunit binding domain…x-ray diffractionI, J——
1W85The crystal structure of pyruvate dehydrogenase E1 bound to the peripheral subunit binding domain…x-ray diffractionI, J——
1W88The crystal structure of pyruvate dehydrogenase E1(D180N,E183Q) bound to the peripheral subunit…x-ray diffractionI, J——
1W88The crystal structure of pyruvate dehydrogenase E1(D180N,E183Q) bound to the peripheral subunit…x-ray diffractionI, J——
2PDDThe high resolution structure of the peripheral subunit-binding domain of dihydrolipoamide…solution nmrA——
2PDDThe high resolution structure of the peripheral subunit-binding domain of dihydrolipoamide…solution nmrA——
2PDEThe high resolution structure of the peripheral subunit-binding domain of dihydrolipoamide…solution nmrA——
2PDEThe high resolution structure of the peripheral subunit-binding domain of dihydrolipoamide…solution nmrA——
3DUFSnapshots of catalysis in the E1 subunit of the pyruvate dehydrogenase multi-enzyme complexx-ray diffractionI, J——
3DUFSnapshots of catalysis in the E1 subunit of the pyruvate dehydrogenase multi-enzyme complexx-ray diffractionI, J——
3DV0Snapshots of catalysis in the E1 subunit of the pyruvate dehydrogenase multi-enzyme complexx-ray diffractionI, J——
3DV0Snapshots of catalysis in the E1 subunit of the pyruvate dehydrogenase multi-enzyme complexx-ray diffractionI, J——
3DVASnapshots of catalysis in the E1 subunit of the pyruvate dehydrogenase multi-enzyme complexx-ray diffractionI, J——
3DVASnapshots of catalysis in the E1 subunit of the pyruvate dehydrogenase multi-enzyme complexx-ray diffractionI, J——
P11961AlphaFold monomer V2.0 prediction for dihydrolipoyllysine-residue acetyltransferase component of…———

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