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6S59

Structure of ovine transhydrogenase in the apo state

Functional Information from GO Data
ChainGOidnamespacecontents
A0016491molecular_functionoxidoreductase activity
A1902600biological_processproton transmembrane transport
B0016491molecular_functionoxidoreductase activity
B1902600biological_processproton transmembrane transport
Functional Information from PDB Data
site_idAC1
Number of Residues5
Detailsbinding site for residue PC1 A 1101
ChainResidue
ATYR470
ATRP474
AILE828
ATYR831
APC11102

site_idAC2
Number of Residues7
Detailsbinding site for residue PC1 A 1102
ChainResidue
APC11101
BLEU586
BALA593
ATYR436
APHE462
AILE467
ATYR470

site_idAC3
Number of Residues6
Detailsbinding site for residue PC1 A 1103
ChainResidue
ATYR798
ATYR831
ACYS834
AARG839
ASER840
ALEU841

site_idAC4
Number of Residues3
Detailsbinding site for residue PC1 A 1104
ChainResidue
AGLN536
AASN552
AMET609

site_idAC5
Number of Residues8
Detailsbinding site for residue PC1 B 1101
ChainResidue
BPHE462
BTYR470
BTRP474
BTRP801
BSER824
BTYR831
BPC11102
BPC11103

site_idAC6
Number of Residues5
Detailsbinding site for residue PC1 B 1102
ChainResidue
ALEU586
BTYR436
BTYR470
BHIS471
BPC11101

site_idAC7
Number of Residues4
Detailsbinding site for residue PC1 B 1103
ChainResidue
BTYR798
BTYR831
BSER840
BPC11101

site_idAC8
Number of Residues4
Detailsbinding site for residue PC1 B 1104
ChainResidue
BGLN536
BASP540
BASN552
BALA559

Functional Information from PROSITE/UniProt
site_idPS00836
Number of Residues27
DetailsALADH_PNT_1 Alanine dehydrogenase & pyridine nucleotide transhydrogenase signature 1. GVPkEifqNEk..RVAlSPaGVqaLvKqG
ChainResidueDetails
AGLY17-GLY43

site_idPS00837
Number of Residues26
DetailsALADH_PNT_2 Alanine dehydrogenase & pyridine nucleotide transhydrogenase signature 2. IVGGGvAGlaSagaAkSMGAiVrgfD
ChainResidueDetails
AILE189-ASP214

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues550
DetailsTransmembrane: {"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues32
DetailsTopological domain: {"description":"Mitochondrial matrix","evidences":[{"source":"UniProtKB","id":"P11024","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues32
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"source":"UniProtKB","id":"P11024","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues30
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"31462775","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6QTI","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6QUE","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"31462775","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6QUE","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P07001","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues6
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"Q13423","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues4
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q13423","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues10
DetailsModified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"Q61941","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

247536

PDB entries from 2026-01-14

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