Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1OGP

The crystal structure of plant sulfite oxidase provides insight into sulfite oxidation in plants and animals

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005739	cellular_component	mitochondrion
A	0005777	cellular_component	peroxisome
A	0005829	cellular_component	cytosol
A	0006790	biological_process	sulfur compound metabolic process
A	0008482	molecular_function	sulfite oxidase activity
A	0010477	biological_process	response to sulfur dioxide
A	0015994	biological_process	chlorophyll metabolic process
A	0016491	molecular_function	oxidoreductase activity
A	0030151	molecular_function	molybdenum ion binding
A	0046872	molecular_function	metal ion binding
B	0005739	cellular_component	mitochondrion
B	0005777	cellular_component	peroxisome
B	0005829	cellular_component	cytosol
B	0006790	biological_process	sulfur compound metabolic process
B	0008482	molecular_function	sulfite oxidase activity
B	0010477	biological_process	response to sulfur dioxide
B	0015994	biological_process	chlorophyll metabolic process
B	0016491	molecular_function	oxidoreductase activity
B	0030151	molecular_function	molybdenum ion binding
B	0046872	molecular_function	metal ion binding
C	0005739	cellular_component	mitochondrion
C	0005777	cellular_component	peroxisome
C	0005829	cellular_component	cytosol
C	0006790	biological_process	sulfur compound metabolic process
C	0008482	molecular_function	sulfite oxidase activity
C	0010477	biological_process	response to sulfur dioxide
C	0015994	biological_process	chlorophyll metabolic process
C	0016491	molecular_function	oxidoreductase activity
C	0030151	molecular_function	molybdenum ion binding
C	0046872	molecular_function	metal ion binding
D	0005739	cellular_component	mitochondrion
D	0005777	cellular_component	peroxisome
D	0005829	cellular_component	cytosol
D	0006790	biological_process	sulfur compound metabolic process
D	0008482	molecular_function	sulfite oxidase activity
D	0010477	biological_process	response to sulfur dioxide
D	0015994	biological_process	chlorophyll metabolic process
D	0016491	molecular_function	oxidoreductase activity
D	0030151	molecular_function	molybdenum ion binding
D	0046872	molecular_function	metal ion binding
E	0005739	cellular_component	mitochondrion
E	0005777	cellular_component	peroxisome
E	0005829	cellular_component	cytosol
E	0006790	biological_process	sulfur compound metabolic process
E	0008482	molecular_function	sulfite oxidase activity
E	0010477	biological_process	response to sulfur dioxide
E	0015994	biological_process	chlorophyll metabolic process
E	0016491	molecular_function	oxidoreductase activity
E	0030151	molecular_function	molybdenum ion binding
E	0046872	molecular_function	metal ion binding
F	0005739	cellular_component	mitochondrion
F	0005777	cellular_component	peroxisome
F	0005829	cellular_component	cytosol
F	0006790	biological_process	sulfur compound metabolic process
F	0008482	molecular_function	sulfite oxidase activity
F	0010477	biological_process	response to sulfur dioxide
F	0015994	biological_process	chlorophyll metabolic process
F	0016491	molecular_function	oxidoreductase activity
F	0030151	molecular_function	molybdenum ion binding
F	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CS A1391

Chain	Residue
A	SER66
A	THR68
A	ASP223

site_id	AC2
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CS A1392

Chain	Residue
A	SER329
A	SER331
A	HOH2090

site_id	AC3
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CS B1391

Chain	Residue
B	SER66
B	THR68
B	ASP223

site_id	AC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CS B1392

Chain	Residue
B	SER329
B	SER330
B	SER331
B	ASP332
B	HOH2073

site_id	AC5
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CS C1391

Chain	Residue
C	SER66
C	THR68
C	ASP223

site_id	AC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CS C1392

Chain	Residue
C	SER329
C	SER331
C	ASP332
C	HOH2070

site_id	AC7
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CS D1391

Chain	Residue
D	SER66
D	THR68
D	ASP223

site_id	AC8
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CS D1392

Chain	Residue
D	SER329
D	SER331
D	HOH2074

site_id	AC9
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CS E1391

Chain	Residue
E	SER66
E	THR68
E	ASP223

site_id	BC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CS E1392

Chain	Residue
E	SER329
E	SER330
E	SER331
E	ASP332

site_id	BC2
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CS F1391

Chain	Residue
F	SER66
F	THR68
F	ASP223

site_id	BC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CS F1392

Chain	Residue
F	SER329
F	SER330
F	SER331
F	ASP332
F	HOH2082

site_id	BC4
Number of Residues	19
Details	BINDING SITE FOR RESIDUE MTQ A1394

Chain	Residue
A	PHE48
A	TYR49
A	ARG51
A	HIS53
A	CYS98
A	ALA99
A	SER159
A	ASP161
A	TYR171
A	ARG207
A	GLY215
A	ALA216
A	SER218
A	VAL219
A	LYS220
A	TRP221
A	TYR241
A	HOH2060
A	HOH2061

site_id	BC5
Number of Residues	19
Details	BINDING SITE FOR RESIDUE MTQ B1394

Chain	Residue
B	PHE48
B	TYR49
B	ARG51
B	ASN52
B	HIS53
B	CYS98
B	ALA99
B	SER159
B	ASP161
B	TYR171
B	HIS202
B	ARG207
B	GLY215
B	ALA216
B	SER218
B	VAL219
B	LYS220
B	TRP221
B	TYR241

site_id	BC6
Number of Residues	18
Details	BINDING SITE FOR RESIDUE MTQ C1394

Chain	Residue
C	TYR49
C	LYS50
C	ARG51
C	ASN52
C	HIS53
C	CYS98
C	ALA99
C	SER159
C	ASP161
C	TYR171
C	HIS202
C	ARG207
C	GLY215
C	ALA216
C	SER218
C	LYS220
C	TRP221
C	TYR241

site_id	BC7
Number of Residues	19
Details	BINDING SITE FOR RESIDUE MTQ D1394

Chain	Residue
D	TYR49
D	ARG51
D	ASN52
D	HIS53
D	CYS98
D	ALA99
D	SER159
D	ASP161
D	TYR171
D	HIS202
D	ARG207
D	GLY215
D	ALA216
D	SER218
D	LYS220
D	TRP221
D	TYR241
D	HOH2090
D	PHE48

site_id	BC8
Number of Residues	16
Details	BINDING SITE FOR RESIDUE MTQ E1394

Chain	Residue
E	TYR49
E	ARG51
E	HIS53
E	CYS98
E	ALA99
E	SER159
E	ASP161
E	TYR171
E	HIS202
E	ARG207
E	GLY215
E	ALA216
E	SER218
E	LYS220
E	TRP221
E	TYR241

site_id	BC9
Number of Residues	20
Details	BINDING SITE FOR RESIDUE MTQ F1394

Chain	Residue
F	PHE48
F	TYR49
F	LYS50
F	ARG51
F	HIS53
F	CYS98
F	ALA99
F	SER159
F	ASP161
F	TYR171
F	HIS202
F	ARG207
F	GLY215
F	ALA216
F	SER218
F	VAL219
F	LYS220
F	TRP221
F	TYR241
F	HOH2111

site_id	CC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE GOL A1393

Chain	Residue
A	SER174
A	ILE175
A	GLU231
A	ARG259
A	MET262
A	HOH2081

site_id	CC2
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL B1393

Chain	Residue
B	HIS154
B	SER174
B	ILE175
B	THR176
B	GLU231
B	ARG259
B	HOH2095

site_id	CC3
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL C1393

Chain	Residue
C	HIS154
C	SER174
C	ILE175
C	THR176
C	GLU231
C	PRO260
C	HOH2086

site_id	CC4
Number of Residues	9
Details	BINDING SITE FOR RESIDUE GOL D1393

Chain	Residue
C	GLU327
C	HOH2068
D	HIS154
D	SER174
D	ILE175
D	THR176
D	GLU231
D	ARG259
D	HOH2089

site_id	CC5
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL E1393

Chain	Residue
E	HIS154
E	SER174
E	ILE175
E	THR176
E	GLU231
E	ARG259
E	HOH2107

site_id	CC6
Number of Residues	6
Details	BINDING SITE FOR RESIDUE GOL F1393

Chain	Residue
F	HIS154
F	SER174
F	ILE175
F	THR176
F	GLU231
F	ARG259

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	36
Details	BINDING:

Chain	Residue	Details
A	TYR49
B	HIS202
B	ARG207
B	SER218
C	TYR49
C	CYS98
C	SER159
C	HIS202
C	ARG207
C	SER218
D	TYR49
A	CYS98
D	CYS98
D	SER159
D	HIS202
D	ARG207
D	SER218
E	TYR49
E	CYS98
E	SER159
E	HIS202
E	ARG207
A	SER159
E	SER218
F	TYR49
F	CYS98
F	SER159
F	HIS202
F	ARG207
F	SER218
A	HIS202
A	ARG207
A	SER218
B	TYR49
B	CYS98
B	SER159

Catalytic Information from CSA

site_id	CSA1
Number of Residues	2
Details	Annotated By Reference To The Literature 1sox

Chain	Residue	Details
A	ARG51
A	TYR241

site_id	CSA2
Number of Residues	2
Details	Annotated By Reference To The Literature 1sox

Chain	Residue	Details
B	ARG51
B	TYR241

site_id	CSA3
Number of Residues	2
Details	Annotated By Reference To The Literature 1sox

Chain	Residue	Details
C	ARG51
C	TYR241

site_id	CSA4
Number of Residues	2
Details	Annotated By Reference To The Literature 1sox

Chain	Residue	Details
D	ARG51
D	TYR241

site_id	CSA5
Number of Residues	2
Details	Annotated By Reference To The Literature 1sox

Chain	Residue	Details
E	ARG51
E	TYR241

site_id	CSA6
Number of Residues	2
Details	Annotated By Reference To The Literature 1sox

Chain	Residue	Details
F	ARG51
F	TYR241

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