Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

2C1D

Crystal structure of SoxXA from P. pantotrophus

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004792	molecular_function	thiosulfate-cyanide sulfurtransferase activity
A	0005506	molecular_function	iron ion binding
A	0008270	molecular_function	zinc ion 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	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	0005506	molecular_function	iron ion binding
C	0008270	molecular_function	zinc ion 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	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	0005506	molecular_function	iron ion binding
E	0008270	molecular_function	zinc ion 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	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	0005506	molecular_function	iron ion binding
G	0008270	molecular_function	zinc ion 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	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	4
Details	BINDING SITE FOR RESIDUE ZN A1293

Chain	Residue
A	ASP70
A	ASP74
A	HIS190
A	ASP266

site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN A1294

Chain	Residue
A	HIS129
A	HEC1291
A	HOH2335
E	HEC1291

site_id	AC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE ZN A1295

Chain	Residue
A	ASP81
A	ASP265
A	HOH2081
A	HOH2306
A	ASP78

site_id	AC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN A1296

Chain	Residue
A	HEC1291
A	HOH2336
E	HIS129
E	HEC1291

site_id	AC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN C1293

Chain	Residue
C	ASP70
C	ASP74
C	HIS190
C	ASP266

site_id	AC6
Number of Residues	3
Details	BINDING SITE FOR RESIDUE ZN C1294

Chain	Residue
C	ASP78
C	ASP81
C	ASP265

site_id	AC7
Number of Residues	3
Details	BINDING SITE FOR RESIDUE ZN C1295

Chain	Residue
C	HIS129
C	HEC1291
G	HEC1291

site_id	AC8
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN E1293

Chain	Residue
E	ASP70
E	ASP74
E	HIS190
E	ASP266

site_id	AC9
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN E1294

Chain	Residue
E	ASP78
E	ASP81
E	ASP265
E	HOH2327

site_id	BC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN G1293

Chain	Residue
G	ASP70
G	ASP74
G	HIS190
G	ASP266

site_id	BC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE ZN G1294

Chain	Residue
C	HEC1291
G	GLU128
G	HIS129
G	HEC1291
G	HOH2332

site_id	BC3
Number of Residues	3
Details	BINDING SITE FOR RESIDUE ZN G1295

Chain	Residue
G	ASP78
G	ASP81
G	ASP265

site_id	BC4
Number of Residues	22
Details	BINDING SITE FOR RESIDUE HEC A1291

Chain	Residue
A	SER105
A	CYS106
A	CYS109
A	HIS110
A	ARG125
A	HIS129
A	TYR139
A	CYS143
A	ARG147
A	MET148
A	MET163
A	ZN1294
A	ZN1296
A	HOH2156
A	HOH2330
A	HOH2336
E	CYS109
E	HIS110
E	GLU128
E	HIS129
E	HEC1291
E	HOH2146

site_id	BC5
Number of Residues	22
Details	BINDING SITE FOR RESIDUE HEC A1292

Chain	Residue
A	GLY64
A	ARG68
A	SER205
A	CYS206
A	CYS209
A	HIS210
A	ILE218
A	ASP221
A	HIS222
A	LEU223
A	SER224
A	GLY226
A	GLN227
A	ILE228
A	ARG247
A	PHE248
A	CSS251
A	ARG289
A	HOH2266
A	HOH2332
A	HOH2333
A	HOH2334

site_id	BC6
Number of Residues	18
Details	BINDING SITE FOR RESIDUE HEC B1158

Chain	Residue
B	TRP90
B	ILE98
B	PHE106
B	THR109
B	MET111
B	PRO112
B	PHE114
B	VAL148
B	HOH2123
B	HOH2176
A	MET204
B	GLY59
B	CYS61
B	CYS64
B	HIS65
B	ALA80
B	LEU83
B	ARG89

site_id	BC7
Number of Residues	23
Details	BINDING SITE FOR RESIDUE HEC C1291

Chain	Residue
C	SER105
C	CYS106
C	CYS109
C	HIS110
C	MET116
C	ARG125
C	HIS129
C	TYR139
C	CYS143
C	ARG147
C	MET148
C	MET163
C	ZN1295
C	HOH2175
C	HOH2352
C	HOH2353
G	CYS109
G	HIS110
G	GLU128
G	HIS129
G	HEC1291
G	ZN1294
G	HOH2143

site_id	BC8
Number of Residues	24
Details	BINDING SITE FOR RESIDUE HEC C1292

Chain	Residue
C	GLY64
C	ARG68
C	SER205
C	CYS206
C	CYS209
C	HIS210
C	ILE218
C	ASP221
C	HIS222
C	LEU223
C	SER224
C	GLY226
C	GLN227
C	ILE228
C	ARG247
C	PHE248
C	CSS251
C	VAL252
C	ARG289
C	HOH2294
C	HOH2317
C	HOH2354
C	HOH2355
C	HOH2356

site_id	BC9
Number of Residues	18
Details	BINDING SITE FOR RESIDUE HEC D1158

Chain	Residue
C	MET204
D	GLY59
D	CYS61
D	CYS64
D	HIS65
D	ALA80
D	LEU83
D	ARG89
D	TRP90
D	ILE98
D	THR109
D	MET111
D	PRO112
D	PHE114
D	VAL148
D	HOH2140
D	HOH2205
D	HOH2206

site_id	CC1
Number of Residues	22
Details	BINDING SITE FOR RESIDUE HEC E1291

Chain	Residue
A	CYS109
A	HIS110
A	GLU128
A	HIS129
A	HEC1291
A	ZN1294
A	ZN1296
A	HOH2139
E	SER105
E	CYS106
E	CYS109
E	HIS110
E	MET116
E	ARG125
E	HIS129
E	TYR139
E	CYS143
E	ARG147
E	MET148
E	MET163
E	HOH2343
E	HOH2344

site_id	CC2
Number of Residues	22
Details	BINDING SITE FOR RESIDUE HEC E1292

Chain	Residue
E	GLY64
E	ARG68
E	SER205
E	CYS206
E	CYS209
E	HIS210
E	ASP221
E	HIS222
E	LEU223
E	SER224
E	GLY226
E	GLN227
E	ILE228
E	ARG247
E	PHE248
E	CSS251
E	ARG289
E	HOH2308
E	HOH2345
E	HOH2347
E	HOH2348
E	HOH2349

site_id	CC3
Number of Residues	19
Details	BINDING SITE FOR RESIDUE HEC F1158

Chain	Residue
E	MET204
F	GLY59
F	CYS61
F	CYS64
F	HIS65
F	ALA80
F	LEU83
F	ARG89
F	TRP90
F	ILE98
F	PHE110
F	MET111
F	PRO112
F	PHE114
F	VAL148
F	HOH2187
F	HOH2188
F	HOH2190
F	HOH2191

site_id	CC4
Number of Residues	22
Details	BINDING SITE FOR RESIDUE HEC G1291

Chain	Residue
C	CYS109
C	HIS110
C	GLU128
C	HIS129
C	HEC1291
C	ZN1295
G	SER105
G	CYS106
G	CYS109
G	HIS110
G	MET116
G	ARG125
G	HIS129
G	TYR139
G	CYS143
G	ARG147
G	MET148
G	MET163
G	ZN1294
G	HOH2159
G	HOH2177
G	HOH2328

site_id	CC5
Number of Residues	23
Details	BINDING SITE FOR RESIDUE HEC G1292

Chain	Residue
G	GLY64
G	ARG68
G	MET204
G	SER205
G	CYS206
G	CYS209
G	HIS210
G	ASP221
G	HIS222
G	LEU223
G	SER224
G	GLY226
G	GLN227
G	ILE228
G	ARG247
G	PHE248
G	CSS251
G	VAL252
G	ARG289
G	HOH2275
G	HOH2329
G	HOH2330
G	HOH2331

site_id	CC6
Number of Residues	19
Details	BINDING SITE FOR RESIDUE HEC H1158

Chain	Residue
G	MET204
H	GLY59
H	CYS61
H	CYS64
H	HIS65
H	ALA80
H	LEU83
H	ARG89
H	TRP90
H	ILE98
H	PHE106
H	THR109
H	PHE110
H	MET111
H	PRO112
H	PHE114
H	VAL148
H	HOH2200
H	HOH2201

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	ACT_SITE: Cysteine persulfide intermediate => ECO:0000269\|PubMed:16297640

Chain	Residue	Details
A	CSS251
C	CSS251
E	CSS251
G	CSS251

site_id	SWS_FT_FI2
Number of Residues	16
Details	BINDING: BINDING => ECO:0000269\|PubMed:16297640

Chain	Residue	Details
A	ASP78
E	ASP81
E	HIS190
E	ASP266
G	ASP78
G	ASP81
G	HIS190
G	ASP266
A	ASP81
A	HIS190
A	ASP266
C	ASP78
C	ASP81
C	HIS190
C	ASP266
E	ASP78

site_id	SWS_FT_FI3
Number of Residues	12
Details	BINDING: covalent => ECO:0000255\|PROSITE-ProRule:PRU00433, ECO:0000269\|PubMed:16297640

Chain	Residue	Details
A	CYS106
G	CYS106
G	CYS109
G	CYS206
A	CYS109
A	CYS206
C	CYS106
C	CYS109
C	CYS206
E	CYS106
E	CYS109
E	CYS206

site_id	SWS_FT_FI4
Number of Residues	16
Details	BINDING: axial binding residue => ECO:0000255\|PROSITE-ProRule:PRU00433, ECO:0000269\|PubMed:16297640

Chain	Residue	Details
A	HIS110
E	CYS143
E	HIS210
E	CSS251
G	HIS110
G	CYS143
G	HIS210
G	CSS251
A	CYS143
A	HIS210
A	CSS251
C	HIS110
C	CYS143
C	HIS210
C	CSS251
E	HIS110

site_id	SWS_FT_FI5
Number of Residues	4
Details	BINDING: covalent => ECO:0000250\|UniProtKB:Q939U1, ECO:0000255\|PROSITE-ProRule:PRU00433

Chain	Residue	Details
A	CYS209
C	CYS209
E	CYS209
G	CYS209

site_id	SWS_FT_FI6
Number of Residues	4
Details	BINDING: BINDING => ECO:0000250\|UniProtKB:Q939U1

Chain	Residue	Details
A	ARG247
C	ARG247
E	ARG247
G	ARG247

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