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1X13

Crystal structure of E. coli transhydrogenase domain I

Functional Information from GO Data
ChainGOidnamespacecontents
A0016491molecular_functionoxidoreductase activity
A1902600biological_processproton transmembrane transport
B0016491molecular_functionoxidoreductase activity
B1902600biological_processproton transmembrane transport
Functional Information from PROSITE/UniProt
site_idPS00836
Number of Residues27
DetailsALADH_PNT_1 Alanine dehydrogenase & pyridine nucleotide transhydrogenase signature 1. GIPrErltNEt..RVAaTPkTVeqLlKlG
ChainResidueDetails
AGLY1004-GLY1030

site_idPS00837
Number of Residues26
DetailsALADH_PNT_2 Alanine dehydrogenase & pyridine nucleotide transhydrogenase signature 2. VIGAGvAGlaAigaAnSLGAiVrafD
ChainResidueDetails
AVAL1170-ASP1195

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues14
DetailsBinding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"MAY-2005","submissionDatabase":"PDB data bank","title":"Structure determination of a transient complex by NMR using paramagnetic distance restraints - the complex of the soluble domains of Escherichia coli transhydrogenase.","authors":["Johansson T.","Pedersen A.","Leckner J.","Karlsson B.G."]}}]}
ChainResidueDetails

239149

PDB entries from 2025-07-23

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