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 | 0009507 | cellular_component | chloroplast |
| A | 0010477 | biological_process | response to sulfur dioxide |
| A | 0015994 | biological_process | chlorophyll metabolic process |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0020037 | molecular_function | heme binding |
| A | 0030151 | molecular_function | molybdenum ion binding |
| A | 0043546 | molecular_function | molybdopterin cofactor 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 | 0009507 | cellular_component | chloroplast |
| B | 0010477 | biological_process | response to sulfur dioxide |
| B | 0015994 | biological_process | chlorophyll metabolic process |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0020037 | molecular_function | heme binding |
| B | 0030151 | molecular_function | molybdenum ion binding |
| B | 0043546 | molecular_function | molybdopterin cofactor 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 | 0009507 | cellular_component | chloroplast |
| C | 0010477 | biological_process | response to sulfur dioxide |
| C | 0015994 | biological_process | chlorophyll metabolic process |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0020037 | molecular_function | heme binding |
| C | 0030151 | molecular_function | molybdenum ion binding |
| C | 0043546 | molecular_function | molybdopterin cofactor 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 | 0009507 | cellular_component | chloroplast |
| D | 0010477 | biological_process | response to sulfur dioxide |
| D | 0015994 | biological_process | chlorophyll metabolic process |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0020037 | molecular_function | heme binding |
| D | 0030151 | molecular_function | molybdenum ion binding |
| D | 0043546 | molecular_function | molybdopterin cofactor 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 | 0009507 | cellular_component | chloroplast |
| E | 0010477 | biological_process | response to sulfur dioxide |
| E | 0015994 | biological_process | chlorophyll metabolic process |
| E | 0016491 | molecular_function | oxidoreductase activity |
| E | 0020037 | molecular_function | heme binding |
| E | 0030151 | molecular_function | molybdenum ion binding |
| E | 0043546 | molecular_function | molybdopterin cofactor 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 | 0009507 | cellular_component | chloroplast |
| F | 0010477 | biological_process | response to sulfur dioxide |
| F | 0015994 | biological_process | chlorophyll metabolic process |
| F | 0016491 | molecular_function | oxidoreductase activity |
| F | 0020037 | molecular_function | heme binding |
| F | 0030151 | molecular_function | molybdenum ion binding |
| F | 0043546 | molecular_function | molybdopterin cofactor binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CS A 1391 |
| Chain | Residue |
| A | SER66 |
| A | THR68 |
| A | ASP223 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CS A 1392 |
| Chain | Residue |
| A | SER329 |
| A | SER331 |
| A | HOH2090 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CS B 1391 |
| Chain | Residue |
| B | SER66 |
| B | THR68 |
| B | ASP223 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CS B 1392 |
| 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 C 1391 |
| Chain | Residue |
| C | SER66 |
| C | THR68 |
| C | ASP223 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CS C 1392 |
| Chain | Residue |
| C | SER329 |
| C | SER331 |
| C | ASP332 |
| C | HOH2070 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CS D 1391 |
| Chain | Residue |
| D | SER66 |
| D | THR68 |
| D | ASP223 |
| site_id | AC8 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CS D 1392 |
| Chain | Residue |
| D | SER329 |
| D | SER331 |
| D | HOH2074 |
| site_id | AC9 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CS E 1391 |
| Chain | Residue |
| E | SER66 |
| E | THR68 |
| E | ASP223 |
| site_id | BC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CS E 1392 |
| Chain | Residue |
| E | SER329 |
| E | SER330 |
| E | SER331 |
| E | ASP332 |
| site_id | BC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CS F 1391 |
| Chain | Residue |
| F | SER66 |
| F | THR68 |
| F | ASP223 |
| site_id | BC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CS F 1392 |
| 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 A 1394 |
| 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 B 1394 |
| 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 C 1394 |
| 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 D 1394 |
| 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 E 1394 |
| 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 F 1394 |
| 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 A 1393 |
| 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 B 1393 |
| 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 C 1393 |
| 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 D 1393 |
| 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 E 1393 |
| 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 F 1393 |
| 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 | 1392 |
| Details | Region: {"description":"Moco domain"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 66 |
| Details | Binding site: {} |
| Chain | Residue | Details |
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 |
