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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 Residues1304
DetailsTOPO_DOM: Mitochondrial matrix => ECO:0000250|UniProtKB:P11024
ChainResidueDetails
ACYS1-THR431
AGLN536-ASN552
AMET837-LYS1043
BCYS1-THR431
BGLN536-ASN552
BMET837-LYS1043

site_idSWS_FT_FI2
Number of Residues550
DetailsTRANSMEM: Helical => ECO:0000255
ChainResidueDetails
ASER432-ALA450
AILE697-TYR717
AHIS735-MET754
APHE758-GLY776
AVAL790-LEU810
ALEU814-ALA836
BSER432-ALA450
BMET458-PRO478
BLEU484-MET503
BGLY515-THR535
BTYR553-GLY573
AMET458-PRO478
BILE579-GLY599
BLEU603-LEU623
BLEU629-ALA648
BLEU659-TYR679
BILE697-TYR717
BHIS735-MET754
BPHE758-GLY776
BVAL790-LEU810
BLEU814-ALA836
ALEU484-MET503
AGLY515-THR535
ATYR553-GLY573
AILE579-GLY599
ALEU603-LEU623
ALEU629-ALA648
ALEU659-TYR679

site_idSWS_FT_FI3
Number of Residues32
DetailsTOPO_DOM: Cytoplasmic => ECO:0000250|UniProtKB:P11024
ChainResidueDetails
AILE680-LYS696
BILE680-LYS696

site_idSWS_FT_FI4
Number of Residues14
DetailsBINDING: BINDING => ECO:0000269|PubMed:31462775, ECO:0007744|PDB:6QTI, ECO:0007744|PDB:6QUE
ChainResidueDetails
AARG139
BGLY244
BLEU276
BVAL922
BGLY964
BLYS999
AASP214
AGLY244
ALEU276
AVAL922
AGLY964
ALYS999
BARG139
BASP214

site_idSWS_FT_FI5
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:31462775, ECO:0007744|PDB:6QUE
ChainResidueDetails
AVAL194
BVAL194

site_idSWS_FT_FI6
Number of Residues2
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P07001
ChainResidueDetails
AGLU257
BGLU257

site_idSWS_FT_FI7
Number of Residues6
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:Q13423
ChainResidueDetails
ATYR890
AGLY983
AASP1025
BTYR890
BGLY983
BASP1025

site_idSWS_FT_FI8
Number of Residues4
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:Q13423
ChainResidueDetails
ALYS27
ALYS354
BLYS27
BLYS354

site_idSWS_FT_FI9
Number of Residues10
DetailsMOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:Q61941
ChainResidueDetails
ALYS74
BLYS1036
ALYS181
ALYS251
ALYS288
ALYS1036
BLYS74
BLYS181
BLYS251
BLYS288

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PDB entries from 2024-07-17

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