Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1H31

Oxidised SoxAX complex from Rhodovulum sulfidophilum

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004792	molecular_function	thiosulfate-cyanide sulfurtransferase activity
A	0005515	molecular_function	protein binding
A	0009055	molecular_function	electron transfer activity
A	0016491	molecular_function	oxidoreductase activity
A	0016669	molecular_function	oxidoreductase activity, acting on a sulfur group of donors, cytochrome as acceptor
A	0016740	molecular_function	transferase activity
A	0016783	molecular_function	sulfurtransferase activity
A	0019417	biological_process	sulfur oxidation
A	0019418	biological_process	sulfide oxidation
A	0020037	molecular_function	heme binding
A	0042597	cellular_component	periplasmic space
A	0046872	molecular_function	metal ion binding
A	0046982	molecular_function	protein heterodimerization activity
A	0070069	cellular_component	cytochrome complex
B	0009055	molecular_function	electron transfer activity
B	0020037	molecular_function	heme binding
C	0004792	molecular_function	thiosulfate-cyanide sulfurtransferase activity
C	0005515	molecular_function	protein binding
C	0009055	molecular_function	electron transfer activity
C	0016491	molecular_function	oxidoreductase activity
C	0016669	molecular_function	oxidoreductase activity, acting on a sulfur group of donors, cytochrome as acceptor
C	0016740	molecular_function	transferase activity
C	0016783	molecular_function	sulfurtransferase activity
C	0019417	biological_process	sulfur oxidation
C	0019418	biological_process	sulfide oxidation
C	0020037	molecular_function	heme binding
C	0042597	cellular_component	periplasmic space
C	0046872	molecular_function	metal ion binding
C	0046982	molecular_function	protein heterodimerization activity
C	0070069	cellular_component	cytochrome complex
D	0009055	molecular_function	electron transfer activity
D	0020037	molecular_function	heme binding
E	0004792	molecular_function	thiosulfate-cyanide sulfurtransferase activity
E	0005515	molecular_function	protein binding
E	0009055	molecular_function	electron transfer activity
E	0016491	molecular_function	oxidoreductase activity
E	0016669	molecular_function	oxidoreductase activity, acting on a sulfur group of donors, cytochrome as acceptor
E	0016740	molecular_function	transferase activity
E	0016783	molecular_function	sulfurtransferase activity
E	0019417	biological_process	sulfur oxidation
E	0019418	biological_process	sulfide oxidation
E	0020037	molecular_function	heme binding
E	0042597	cellular_component	periplasmic space
E	0046872	molecular_function	metal ion binding
E	0046982	molecular_function	protein heterodimerization activity
E	0070069	cellular_component	cytochrome complex
F	0009055	molecular_function	electron transfer activity
F	0020037	molecular_function	heme binding
G	0004792	molecular_function	thiosulfate-cyanide sulfurtransferase activity
G	0005515	molecular_function	protein binding
G	0009055	molecular_function	electron transfer activity
G	0016491	molecular_function	oxidoreductase activity
G	0016669	molecular_function	oxidoreductase activity, acting on a sulfur group of donors, cytochrome as acceptor
G	0016740	molecular_function	transferase activity
G	0016783	molecular_function	sulfurtransferase activity
G	0019417	biological_process	sulfur oxidation
G	0019418	biological_process	sulfide oxidation
G	0020037	molecular_function	heme binding
G	0042597	cellular_component	periplasmic space
G	0046872	molecular_function	metal ion binding
G	0046982	molecular_function	protein heterodimerization activity
G	0070069	cellular_component	cytochrome complex
H	0009055	molecular_function	electron transfer activity
H	0020037	molecular_function	heme binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	18
Details	BINDING SITE FOR RESIDUE HEC A 1262

Chain	Residue
A	ALA75
A	CYS114
A	ARG118
A	MET119
A	HOH2117
A	HOH2118
A	HOH2119
A	HOH2120
H	THR109
H	LYS111
A	CYS76
A	CYS79
A	HIS80
A	LEU90
A	TYR94
A	SER100
A	MET110
A	ILE111

site_id	AC2
Number of Residues	21
Details	BINDING SITE FOR RESIDUE HEC A 1263

Chain	Residue
A	GLY34
A	ARG38
A	SER176
A	CYS177
A	CYS180
A	HIS181
A	ASP192
A	HIS193
A	LEU194
A	SER195
A	GLY197
A	GLN198
A	ILE199
A	PHE202
A	PHE219
A	CSS222
A	ARG260
A	HOH2092
A	HOH2097
A	HOH2122
A	HOH2123

site_id	AC3
Number of Residues	19
Details	BINDING SITE FOR RESIDUE HEC B 1139

Chain	Residue
A	TYR184
B	GLY40
B	ASN41
B	CYS42
B	CYS45
B	HIS46
B	PRO62
B	LEU64
B	ARG70
B	TYR71
B	LEU80
B	PHE87
B	THR90
B	VAL91
B	MET92
B	PRO93
B	TYR95
B	VAL129
B	HOH2050

site_id	AC4
Number of Residues	15
Details	BINDING SITE FOR RESIDUE HEC C 1262

Chain	Residue
C	ALA75
C	CYS76
C	CYS79
C	HIS80
C	LEU90
C	TYR94
C	SER100
C	MET110
C	ILE111
C	CYS114
C	ARG118
C	MET119
C	HOH2098
C	HOH2099
C	HOH2100

site_id	AC5
Number of Residues	21
Details	BINDING SITE FOR RESIDUE HEC C 1263

Chain	Residue
C	GLY34
C	ARG38
C	SER176
C	CYS177
C	CYS180
C	HIS181
C	ILE189
C	ASP192
C	HIS193
C	LEU194
C	SER195
C	GLN198
C	ILE199
C	PHE202
C	PHE219
C	CSS222
C	ILE223
C	ARG260
C	HOH2089
C	HOH2101
C	HOH2102

site_id	AC6
Number of Residues	21
Details	BINDING SITE FOR RESIDUE HEC D 1139

Chain	Residue
D	HIS46
D	GLY61
D	PRO62
D	LEU64
D	ARG70
D	TYR71
D	ILE79
D	LEU80
D	PHE87
D	THR90
D	VAL91
D	MET92
D	TYR95
D	HOH2047
D	HOH2048
D	HOH2050
C	TYR184
D	GLY40
D	ASN41
D	CYS42
D	CYS45

site_id	AC7
Number of Residues	15
Details	BINDING SITE FOR RESIDUE HEC E 1262

Chain	Residue
B	GLU114
E	ALA75
E	CYS76
E	CYS79
E	HIS80
E	LEU90
E	TYR94
E	SER100
E	MET110
E	ILE111
E	CYS114
E	ARG118
E	MET119
E	HOH2055
E	HOH2124

site_id	AC8
Number of Residues	24
Details	BINDING SITE FOR RESIDUE HEC E 1263

Chain	Residue
E	GLY34
E	ARG38
E	LEU175
E	SER176
E	CYS177
E	CYS180
E	HIS181
E	ASP192
E	HIS193
E	LEU194
E	SER195
E	GLY197
E	GLN198
E	ILE199
E	PHE202
E	ARG218
E	PHE219
E	CSS222
E	ARG260
E	HOH2015
E	HOH2090
E	HOH2122
E	HOH2125
E	HOH2126

site_id	AC9
Number of Residues	18
Details	BINDING SITE FOR RESIDUE HEC F 1139

Chain	Residue
E	TYR184
E	HOH2083
F	CYS42
F	CYS45
F	HIS46
F	GLY61
F	PRO62
F	ARG70
F	TYR71
F	LEU80
F	PHE87
F	THR90
F	VAL91
F	MET92
F	PRO93
F	TYR95
F	VAL129
F	LEU133

site_id	BC1
Number of Residues	17
Details	BINDING SITE FOR RESIDUE HEC G 1262

Chain	Residue
G	ALA75
G	CYS76
G	CYS79
G	HIS80
G	LEU90
G	TYR94
G	SER100
G	MET110
G	ILE111
G	CYS114
G	ARG118
G	MET119
G	HOH2049
G	HOH2055
G	HOH2109
G	HOH2110
G	HOH2111

site_id	BC2
Number of Residues	22
Details	BINDING SITE FOR RESIDUE HEC G 1263

Chain	Residue
G	GLY34
G	ARG38
G	LEU175
G	SER176
G	CYS177
G	CYS180
G	HIS181
G	ASP192
G	HIS193
G	LEU194
G	SER195
G	ILE199
G	PHE202
G	ARG218
G	PHE219
G	CSS222
G	ILE223
G	ARG260
G	HOH2108
G	HOH2112
G	HOH2113
G	HOH2114

site_id	BC3
Number of Residues	19
Details	BINDING SITE FOR RESIDUE HEC H 1139

Chain	Residue
G	TYR184
H	CYS42
H	CYS45
H	HIS46
H	GLY61
H	PRO62
H	LEU64
H	ARG70
H	TYR71
H	LEU80
H	PHE87
H	THR90
H	VAL91
H	MET92
H	PRO93
H	TYR95
H	VAL129
H	LEU133
H	HOH2065

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	376
Details	Domain: {"description":"Cytochrome c","evidences":[{"source":"PROSITE-ProRule","id":"PRU00433","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	4
Details	Active site: {"description":"Cysteine persulfide intermediate","evidences":[{"source":"PubMed","id":"12411478","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23060437","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	16
Details	Binding site: {"description":"covalent","evidences":[{"source":"PROSITE-ProRule","id":"PRU00433","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"12411478","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23060437","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	16
Details	Binding site: {"description":"axial binding residue","evidences":[{"source":"PROSITE-ProRule","id":"PRU00433","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"12411478","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23060437","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"PubMed","id":"12411478","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)