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1H33

Oxidised SoxAX complex from Rhodovulum sulfidophilum

Functional Information from GO Data
ChainGOidnamespacecontents
A0004792molecular_functionthiosulfate sulfurtransferase activity
A0005515molecular_functionprotein binding
A0009055molecular_functionelectron transfer activity
A0016491molecular_functionoxidoreductase activity
A0016669molecular_functionoxidoreductase activity, acting on a sulfur group of donors, cytochrome as acceptor
A0016740molecular_functiontransferase activity
A0016783molecular_functionsulfurtransferase activity
A0019417biological_processsulfur oxidation
A0019418biological_processsulfide oxidation
A0020037molecular_functionheme binding
A0042597cellular_componentperiplasmic space
A0046872molecular_functionmetal ion binding
A0046982molecular_functionprotein heterodimerization activity
A0070069cellular_componentcytochrome complex
B0009055molecular_functionelectron transfer activity
B0020037molecular_functionheme binding
Functional Information from PDB Data
site_idAC1
Number of Residues13
DetailsBINDING SITE FOR RESIDUE HEC A1262
ChainResidue
AALA75
AMET119
AHOH2266
AHOH2267
BPHE56
ACYS76
ACYS79
AHIS80
ALEU90
ATYR94
ASER100
ACYS114
AARG118

site_idAC2
Number of Residues21
DetailsBINDING SITE FOR RESIDUE HEC A1263
ChainResidue
AGLY34
AARG38
ASER176
ACYS177
ACYS180
AHIS181
AILE189
AHIS193
ASER195
AGLY197
AGLN198
AILE199
APHE202
AARG218
APHE219
ACSS222
AARG260
AHOH2218
AHOH2268
AHOH2269
AHOH2270

site_idAC3
Number of Residues18
DetailsBINDING SITE FOR RESIDUE HEC B1138
ChainResidue
BGLY40
BCYS42
BCYS45
BHIS46
BPRO62
BLEU64
BARG70
BTYR71
BILE79
BLEU80
BPHE87
BTHR90
BVAL91
BMET92
BTYR95
BVAL129
BHOH2082
BHOH2083

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Cysteine persulfide intermediate => ECO:0000269|PubMed:12411478, ECO:0000269|PubMed:23060437
ChainResidueDetails
ACSS222

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: covalent => ECO:0000255|PROSITE-ProRule:PRU00433, ECO:0000269|PubMed:12411478, ECO:0000269|PubMed:23060437
ChainResidueDetails
ACYS76
ACYS79
ACYS177
ACYS180

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: axial binding residue => ECO:0000255|PROSITE-ProRule:PRU00433, ECO:0000269|PubMed:12411478, ECO:0000269|PubMed:23060437
ChainResidueDetails
AHIS80
ACYS114
AHIS181
ACSS222

site_idSWS_FT_FI4
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:12411478
ChainResidueDetails
AARG218

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PDB entries from 2024-06-26

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