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6SDR

W-formate dehydrogenase from Desulfovibrio vulgaris - Oxidized form

Functional Information from GO Data
ChainGOidnamespacecontents
A0005515molecular_functionprotein binding
A0008863molecular_functionformate dehydrogenase (NAD+) activity
A0009055molecular_functionelectron transfer activity
A0009061biological_processanaerobic respiration
A0016491molecular_functionoxidoreductase activity
A0030151molecular_functionmolybdenum ion binding
A0042597cellular_componentperiplasmic space
A0043546molecular_functionmolybdopterin cofactor binding
A0045333biological_processcellular respiration
A0046872molecular_functionmetal ion binding
A0047111molecular_functionformate dehydrogenase (cytochrome-c-553) activity
A0051536molecular_functioniron-sulfur cluster binding
A0051539molecular_function4 iron, 4 sulfur cluster binding
B0030313cellular_componentcell envelope
B0046872molecular_functionmetal ion binding
B0051536molecular_functioniron-sulfur cluster binding
B0051539molecular_function4 iron, 4 sulfur cluster binding
Functional Information from PDB Data
site_idAC1
Number of Residues35
Detailsbinding site for residue MGD A 1101
ChainResidue
ALYS90
AASP254
APRO255
AARG256
ASER272
AGLY273
AASP275
AALA404
AMET405
AGLY406
ATRP407
ASEC192
AGLY442
ATYR883
AARG884
AVAL885
ATHR886
AHIS888
ATRP889
AGLN890
AHIS965
ALYS996
AMET225
AMGD1102
AH2S1109
AW1110
AHOH1349
AHOH1357
AHOH1379
AGLY226
ASER227
AASN228
AGLU231
AASN232
AVAL253

site_idAC2
Number of Residues32
Detailsbinding site for residue MGD A 1102
ChainResidue
AALA164
AGLN188
AILE191
ASEC192
AMET405
AGLU443
ATRP551
AGLY552
AMET553
AASN554
AGLY558
AASN579
ALEU580
ACYS608
ACYS609
ALYS614
AASP641
ATHR882
AARG884
AGLN890
ATHR891
ALEU893
AMET894
ATRP964
AASN979
ATHR995
ALYS996
AMGD1101
AH2S1109
AW1110
AHOH1260
AHOH1352

site_idAC3
Number of Residues10
Detailsbinding site for residue SF4 A 1103
ChainResidue
ACYS50
ATYR52
ACYS53
AGLY56
ACYS57
ALEU87
ACYS88
ALYS90
APRO234
AILE235

site_idAC4
Number of Residues9
Detailsbinding site for residue GOL A 1104
ChainResidue
AASN228
AGLU231
AARG256
AARG259
AARG884
AGLU911
AARG946
AHOH1349
BHIS39

site_idAC5
Number of Residues11
Detailsbinding site for residue GOL A 1105
ChainResidue
ATYR300
AARG775
AVAL778
AASP779
ALYS780
APRO810
AGLY811
ALYS813
AHIS814
APRO815
AHOH1289

site_idAC6
Number of Residues7
Detailsbinding site for residue GOL A 1106
ChainResidue
AGLN447
ATHR450
ATYR462
AGOL1107
AGOL1108
AHIS193
AARG441

site_idAC7
Number of Residues6
Detailsbinding site for residue GOL A 1107
ChainResidue
ASER194
AVAL197
ATHR450
ALEU455
AHIS457
AGOL1106

site_idAC8
Number of Residues8
Detailsbinding site for residue GOL A 1108
ChainResidue
AGLY207
AALA208
ATYR462
ATRP765
AGOL1106
AHOH1268
AHOH1308
AHOH1494

site_idAC9
Number of Residues5
Detailsbinding site for residue H2S A 1109
ChainResidue
ASEC192
AVAL446
AMGD1101
AMGD1102
AW1110

site_idAD1
Number of Residues4
Detailsbinding site for residue W A 1110
ChainResidue
ASEC192
AMGD1101
AMGD1102
AH2S1109

site_idAD2
Number of Residues9
Detailsbinding site for residue SF4 B 301
ChainResidue
BCYS12
BTHR13
BALA14
BCYS15
BARG16
BCYS18
BCYS157
BTHR159
BTHR161

site_idAD3
Number of Residues9
Detailsbinding site for residue SF4 B 302
ChainResidue
BCYS74
BARG75
BCYS77
BPRO81
BCYS82
BVAL103
BCYS121
BPRO126
BLYS137

site_idAD4
Number of Residues10
Detailsbinding site for residue SF4 B 303
ChainResidue
BCYS22
BLYS26
BLYS51
BCYS138
BASP139
BMET140
BCYS141
BPRO151
BALA152
BCYS153

Functional Information from PROSITE/UniProt
site_idPS00551
Number of Residues19
DetailsMOLYBDOPTERIN_PROK_1 Prokaryotic molybdopterin oxidoreductases signature 1. SiCcy.CAVgCgLiVhtakD
ChainResidueDetails
ASER48-ASP66

site_idPS00932
Number of Residues28
DetailsMOLYBDOPTERIN_PROK_3 Prokaryotic molybdopterin oxidoreductases signature 3. AklrGIgNgDtVkVsSlrGaleavAiVT
ChainResidueDetails
AALA917-THR944

246031

PDB entries from 2025-12-10

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