GL1X · GenesisL1 explorer

UniProt A0A383H020

Bifunctional protein PutA (A0A383H020)

Bifunctional protein PutA (UniProt A0A383H020), EC 1.2.1.88, 1.5.5.2: 8 experimental structures on GenesisL1, 6 ligands bound, 17 pockets. Binding sites, pockets, druggability and 3D structures in GL1X.

UniProt
A0A383H020
Protein
Bifunctional protein PutA
EC
1.2.1.88, 1.5.5.2
Experimental structures
8
Predicted models
0
Ligands
6
Pockets
17 · 4 records with a druggable one

Structures

8 records of A0A383H020 in the MolNFT archive: 8 experimental, 0 predicted.

EntryTitleMethodChainsLigandsPockets
7MWTStructure of the E. coli PutA proline dehydrogenase domain (residues 86-630) complexed with…x-ray diffractionAFAD, ZPS, SO45 (best 0.84)
7MWTStructure of the E. COLI puta proline dehydrogenase domain (residues 86-630) complexed with…x-ray diffractionAFAD, ZPS, SO4—
7MWUStructure of the E. coli PutA proline dehydrogenase domain (residues 86-630) complexed with…x-ray diffractionAFAD, ZPM4 (best 0.84)
7MWUStructure of the E. COLI puta proline dehydrogenase domain (residues 86-630) complexed with…x-ray diffractionAFAD, ZPM—
7MWVStructure of the E. coli PutA proline dehydrogenase domain (residues 86-630) complexed with…x-ray diffractionAFAD, ZPJ4 (best 0.84)
7MWVStructure of the E. COLI puta proline dehydrogenase domain (residues 86-630) complexed with…x-ray diffractionAFAD, ZPJ—
7SQNStructure of the E. coli PutA proline dehydrogenase domain (residues 86-630) complexed with…x-ray diffractionAFAD, A8G4 (best 0.83)
7SQNStructure of the E. COLI puta proline dehydrogenase domain (residues 86-630) complexed with…x-ray diffractionAFAD, A8G—

Ligands

  • FAD · Flavin-adenine dinucleotide · in 8 records
  • A8G · (2S)-oxetane-2-carboxylic acid · in 2 records
  • SO4 · Sulfate ion · in 2 records
  • ZPJ · cyclopropanecarboxylic acid · in 2 records
  • ZPM · cyclobutanecarboxylic acid · in 2 records
  • ZPS · cyclobutane-1,1-dicarboxylic acid · in 2 records

Elsewhere

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