Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

4WQ7

Thiosulfate dehydrogenase (TsdA) from Allochromatium vinosum - "as isolated" form

Functional Information from GO Data
ChainGOidnamespacecontents
A0009055molecular_functionelectron transfer activity
A0016491molecular_functionoxidoreductase activity
A0020037molecular_functionheme binding
A0042597cellular_componentperiplasmic space
A0046872molecular_functionmetal ion binding
A0050338molecular_functionthiosulfate dehydrogenase activity
Functional Information from PDB Data
site_idAC1
Number of Residues20
Detailsbinding site for residue HEC A 1001
ChainResidue
ALEU32
ACYS96
APHE97
ASER100
ALEU101
AGLY137
AILE138
AHOH1111
AHOH1168
AHOH1169
AHOH1210
AALA48
AHOH1211
ACYS49
ACYS52
AHIS53
APHE69
AARG75
ALEU89
AARG92

site_idAC2
Number of Residues17
Detailsbinding site for residue HEC A 1002
ChainResidue
AHIS51
APRO54
AARG159
ACYS160
ACYS163
AHIS164
ALEU179
APHE180
APRO181
APRO182
ALEU183
APHE189
APHE204
AILE205
ALYS208
AMET209
AHOH1174

site_idAC3
Number of Residues2
Detailsbinding site for residue IOD A 1004
ChainResidue
AARG82
AGLY194

site_idAC4
Number of Residues2
Detailsbinding site for residue IOD A 1005
ChainResidue
APRO40
AASP41

site_idAC5
Number of Residues6
Detailsbinding site for residue SO4 A 1006
ChainResidue
AASN196
AARG197
AARG197
AGLN198
AHOH1109
AHOH1236

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsBINDING: covalent => ECO:0000255|PROSITE-ProRule:PRU00433
ChainResidueDetails
ACYS49
ACYS52
ACYS160
ACYS163

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: axial binding residue => ECO:0000255|PROSITE-ProRule:PRU00433
ChainResidueDetails
AHIS53
AHIS164

219140

PDB entries from 2024-05-01

PDB statisticsPDBj update infoContact PDBjnumon