1OCR
BOVINE HEART CYTOCHROME C OXIDASE IN THE FULLY REDUCED STATE
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004129 | molecular_function | cytochrome-c oxidase activity |
| A | 0005743 | cellular_component | mitochondrial inner membrane |
| A | 0006119 | biological_process | oxidative phosphorylation |
| A | 0009060 | biological_process | aerobic respiration |
| A | 0016020 | cellular_component | membrane |
| A | 0020037 | molecular_function | heme binding |
| A | 0022904 | biological_process | respiratory electron transport chain |
| A | 0045277 | cellular_component | respiratory chain complex IV |
| A | 0046872 | molecular_function | metal ion binding |
| A | 1902600 | biological_process | proton transmembrane transport |
| B | 0004129 | molecular_function | cytochrome-c oxidase activity |
| B | 0005507 | molecular_function | copper ion binding |
| B | 0005739 | cellular_component | mitochondrion |
| B | 0005743 | cellular_component | mitochondrial inner membrane |
| B | 0016020 | cellular_component | membrane |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0022900 | biological_process | electron transport chain |
| B | 0031966 | cellular_component | mitochondrial membrane |
| B | 0042773 | biological_process | ATP synthesis coupled electron transport |
| B | 0045277 | cellular_component | respiratory chain complex IV |
| B | 0046872 | molecular_function | metal ion binding |
| B | 1902600 | biological_process | proton transmembrane transport |
| C | 0004129 | molecular_function | cytochrome-c oxidase activity |
| C | 0005739 | cellular_component | mitochondrion |
| C | 0005743 | cellular_component | mitochondrial inner membrane |
| C | 0006123 | biological_process | mitochondrial electron transport, cytochrome c to oxygen |
| C | 0008535 | biological_process | respiratory chain complex IV assembly |
| C | 0009055 | molecular_function | electron transfer activity |
| C | 0016020 | cellular_component | membrane |
| C | 0019646 | biological_process | aerobic electron transport chain |
| C | 0022904 | biological_process | respiratory electron transport chain |
| C | 0045277 | cellular_component | respiratory chain complex IV |
| C | 1902600 | biological_process | proton transmembrane transport |
| D | 0006123 | biological_process | mitochondrial electron transport, cytochrome c to oxygen |
| D | 0045277 | cellular_component | respiratory chain complex IV |
| E | 0005743 | cellular_component | mitochondrial inner membrane |
| E | 0006123 | biological_process | mitochondrial electron transport, cytochrome c to oxygen |
| E | 0045277 | cellular_component | respiratory chain complex IV |
| F | 0005740 | cellular_component | mitochondrial envelope |
| F | 0006123 | biological_process | mitochondrial electron transport, cytochrome c to oxygen |
| F | 0045277 | cellular_component | respiratory chain complex IV |
| G | 0005743 | cellular_component | mitochondrial inner membrane |
| H | 0005739 | cellular_component | mitochondrion |
| H | 0005743 | cellular_component | mitochondrial inner membrane |
| H | 0006119 | biological_process | oxidative phosphorylation |
| H | 0016020 | cellular_component | membrane |
| H | 0045277 | cellular_component | respiratory chain complex IV |
| I | 0005743 | cellular_component | mitochondrial inner membrane |
| I | 0006119 | biological_process | oxidative phosphorylation |
| I | 0016020 | cellular_component | membrane |
| I | 0045277 | cellular_component | respiratory chain complex IV |
| J | 0006123 | biological_process | mitochondrial electron transport, cytochrome c to oxygen |
| J | 0045277 | cellular_component | respiratory chain complex IV |
| K | 0006123 | biological_process | mitochondrial electron transport, cytochrome c to oxygen |
| L | 0006123 | biological_process | mitochondrial electron transport, cytochrome c to oxygen |
| L | 0045277 | cellular_component | respiratory chain complex IV |
| M | 0006123 | biological_process | mitochondrial electron transport, cytochrome c to oxygen |
| M | 0045277 | cellular_component | respiratory chain complex IV |
| N | 0004129 | molecular_function | cytochrome-c oxidase activity |
| N | 0005743 | cellular_component | mitochondrial inner membrane |
| N | 0006119 | biological_process | oxidative phosphorylation |
| N | 0009060 | biological_process | aerobic respiration |
| N | 0016020 | cellular_component | membrane |
| N | 0020037 | molecular_function | heme binding |
| N | 0022904 | biological_process | respiratory electron transport chain |
| N | 0045277 | cellular_component | respiratory chain complex IV |
| N | 0046872 | molecular_function | metal ion binding |
| N | 1902600 | biological_process | proton transmembrane transport |
| O | 0004129 | molecular_function | cytochrome-c oxidase activity |
| O | 0005507 | molecular_function | copper ion binding |
| O | 0005739 | cellular_component | mitochondrion |
| O | 0005743 | cellular_component | mitochondrial inner membrane |
| O | 0016020 | cellular_component | membrane |
| O | 0016491 | molecular_function | oxidoreductase activity |
| O | 0022900 | biological_process | electron transport chain |
| O | 0031966 | cellular_component | mitochondrial membrane |
| O | 0042773 | biological_process | ATP synthesis coupled electron transport |
| O | 0045277 | cellular_component | respiratory chain complex IV |
| O | 0046872 | molecular_function | metal ion binding |
| O | 1902600 | biological_process | proton transmembrane transport |
| P | 0004129 | molecular_function | cytochrome-c oxidase activity |
| P | 0005739 | cellular_component | mitochondrion |
| P | 0005743 | cellular_component | mitochondrial inner membrane |
| P | 0006123 | biological_process | mitochondrial electron transport, cytochrome c to oxygen |
| P | 0008535 | biological_process | respiratory chain complex IV assembly |
| P | 0009055 | molecular_function | electron transfer activity |
| P | 0016020 | cellular_component | membrane |
| P | 0019646 | biological_process | aerobic electron transport chain |
| P | 0022904 | biological_process | respiratory electron transport chain |
| P | 0045277 | cellular_component | respiratory chain complex IV |
| P | 1902600 | biological_process | proton transmembrane transport |
| Q | 0006123 | biological_process | mitochondrial electron transport, cytochrome c to oxygen |
| Q | 0045277 | cellular_component | respiratory chain complex IV |
| R | 0005743 | cellular_component | mitochondrial inner membrane |
| R | 0006123 | biological_process | mitochondrial electron transport, cytochrome c to oxygen |
| R | 0045277 | cellular_component | respiratory chain complex IV |
| S | 0005740 | cellular_component | mitochondrial envelope |
| S | 0006123 | biological_process | mitochondrial electron transport, cytochrome c to oxygen |
| S | 0045277 | cellular_component | respiratory chain complex IV |
| T | 0005743 | cellular_component | mitochondrial inner membrane |
| U | 0005739 | cellular_component | mitochondrion |
| U | 0005743 | cellular_component | mitochondrial inner membrane |
| U | 0006119 | biological_process | oxidative phosphorylation |
| U | 0016020 | cellular_component | membrane |
| U | 0045277 | cellular_component | respiratory chain complex IV |
| V | 0005743 | cellular_component | mitochondrial inner membrane |
| V | 0006119 | biological_process | oxidative phosphorylation |
| V | 0016020 | cellular_component | membrane |
| V | 0045277 | cellular_component | respiratory chain complex IV |
| W | 0006123 | biological_process | mitochondrial electron transport, cytochrome c to oxygen |
| W | 0045277 | cellular_component | respiratory chain complex IV |
| X | 0006123 | biological_process | mitochondrial electron transport, cytochrome c to oxygen |
| Y | 0006123 | biological_process | mitochondrial electron transport, cytochrome c to oxygen |
| Y | 0045277 | cellular_component | respiratory chain complex IV |
| Z | 0006123 | biological_process | mitochondrial electron transport, cytochrome c to oxygen |
| Z | 0045277 | cellular_component | respiratory chain complex IV |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CU A 517 |
| Chain | Residue |
| A | HIS240 |
| A | HIS290 |
| A | HIS291 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MG A 518 |
| Chain | Residue |
| A | HIS368 |
| A | ASP369 |
| B | GLU198 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE NA A 519 |
| Chain | Residue |
| A | GLU40 |
| A | GLY45 |
| A | SER441 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CU B 228 |
| Chain | Residue |
| B | HIS161 |
| B | CYS196 |
| B | CYS200 |
| B | MET207 |
| B | CU229 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CU B 229 |
| Chain | Residue |
| B | CYS196 |
| B | GLU198 |
| B | CYS200 |
| B | HIS204 |
| B | CU228 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN F 99 |
| Chain | Residue |
| F | CYS60 |
| F | CYS62 |
| F | CYS82 |
| F | CYS85 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CU N 517 |
| Chain | Residue |
| N | HIS240 |
| N | HIS290 |
| N | HIS291 |
| site_id | AC8 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MG N 518 |
| Chain | Residue |
| N | HIS368 |
| N | ASP369 |
| O | GLU198 |
| site_id | AC9 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE NA N 519 |
| Chain | Residue |
| N | GLU40 |
| N | GLY45 |
| N | SER441 |
| site_id | BC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CU O 228 |
| Chain | Residue |
| O | HIS161 |
| O | CYS196 |
| O | CYS200 |
| O | MET207 |
| O | CU229 |
| site_id | BC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CU O 229 |
| Chain | Residue |
| O | CYS196 |
| O | GLU198 |
| O | CYS200 |
| O | HIS204 |
| O | CU228 |
| site_id | BC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN S 99 |
| Chain | Residue |
| S | CYS60 |
| S | CYS62 |
| S | CYS82 |
| S | CYS85 |
| site_id | BC4 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE HEA A 515 |
| Chain | Residue |
| A | MET28 |
| A | THR31 |
| A | SER34 |
| A | ILE37 |
| A | ARG38 |
| A | TYR54 |
| A | HIS61 |
| A | ALA62 |
| A | MET65 |
| A | VAL70 |
| A | GLY125 |
| A | TRP126 |
| A | TYR371 |
| A | PHE377 |
| A | HIS378 |
| A | SER382 |
| A | MET390 |
| A | PHE393 |
| A | MET417 |
| A | PHE425 |
| A | GLN428 |
| A | ARG438 |
| A | ARG439 |
| site_id | BC5 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE HEA A 516 |
| Chain | Residue |
| A | TRP126 |
| A | TRP236 |
| A | VAL243 |
| A | TYR244 |
| A | HIS290 |
| A | HIS291 |
| A | THR309 |
| A | ILE312 |
| A | ALA313 |
| A | GLY317 |
| A | GLY352 |
| A | GLY355 |
| A | LEU358 |
| A | ALA359 |
| A | ASP364 |
| A | HIS368 |
| A | HIS376 |
| A | PHE377 |
| A | VAL380 |
| A | LEU381 |
| A | ARG438 |
| B | PRO69 |
| site_id | BC6 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE HEA N 515 |
| Chain | Residue |
| N | VAL70 |
| N | GLY125 |
| N | TRP126 |
| N | TYR371 |
| N | PHE377 |
| N | HIS378 |
| N | SER382 |
| N | MET390 |
| N | PHE393 |
| N | MET417 |
| N | PHE425 |
| N | GLN428 |
| N | ARG438 |
| N | ARG439 |
| N | MET28 |
| N | SER34 |
| N | ILE37 |
| N | ARG38 |
| N | TYR54 |
| N | HIS61 |
| N | ALA62 |
| N | MET65 |
| site_id | BC7 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE HEA N 516 |
| Chain | Residue |
| N | TRP126 |
| N | TRP236 |
| N | VAL243 |
| N | TYR244 |
| N | HIS290 |
| N | THR309 |
| N | ILE312 |
| N | ALA313 |
| N | THR316 |
| N | GLY317 |
| N | GLY352 |
| N | GLY355 |
| N | LEU358 |
| N | ALA359 |
| N | ASP364 |
| N | HIS368 |
| N | HIS376 |
| N | PHE377 |
| N | VAL380 |
| N | LEU381 |
| N | ARG438 |
| O | PRO69 |
Functional Information from PROSITE/UniProt
| site_id | PS00077 |
| Number of Residues | 56 |
| Details | COX1_CUB Heme-copper oxidase catalytic subunit, copper B binding region signature. WFFGHPeVyililpgfgmishivtyysgkkepfgymgmvwammsigflgfivwa.HH |
| Chain | Residue | Details |
| A | TRP236-HIS291 |
| site_id | PS00078 |
| Number of Residues | 49 |
| Details | COX2 CO II and nitrous oxide reductase dinuclear copper centers signature. VlHswavpslglktdaipgrlnqttlmssrpglyygq......CseiCgsnHsfM |
| Chain | Residue | Details |
| B | VAL159-MET207 |
| site_id | PS00848 |
| Number of Residues | 23 |
| Details | COX5B_1 Cytochrome c oxidase subunit Vb, zinc binding region signature. VIWfwlhkgeaqrCpsCGthYKL |
| Chain | Residue | Details |
| F | VAL69-LEU91 |
| site_id | PS01329 |
| Number of Residues | 18 |
| Details | COX6A Cytochrome c oxidase subunit VIa signature. IRtKpFsWGDGnHTfFhN |
| Chain | Residue | Details |
| G | ILE55-ASN72 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 150 |
| Details | Topological domain: {"description":"Mitochondrial matrix","evidences":[{"source":"PubMed","id":"2165784","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"27605664","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 152 |
| Details | Transmembrane: {"description":"Helical; Name=I","evidences":[{"source":"PubMed","id":"27605664","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 18 |
| Details | Topological domain: {"description":"Mitochondrial intermembrane","evidences":[{"source":"PubMed","id":"27605664","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8638158","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 174 |
| Details | Transmembrane: {"description":"Helical; Name=II","evidences":[{"source":"PubMed","id":"27605664","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 108 |
| Details | Transmembrane: {"description":"Helical; Name=III","evidences":[{"source":"PubMed","id":"27605664","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 94 |
| Details | Topological domain: {"description":"Mitochondrial intermembrane","evidences":[{"source":"PubMed","id":"2165784","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"27605664","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 104 |
| Details | Transmembrane: {"description":"Helical; Name=IV","evidences":[{"source":"PubMed","id":"27605664","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 112 |
| Details | Transmembrane: {"description":"Helical; Name=V","evidences":[{"source":"PubMed","id":"27605664","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 130 |
| Details | Transmembrane: {"description":"Helical; Name=VI","evidences":[{"source":"PubMed","id":"27605664","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 78 |
| Details | Transmembrane: {"description":"Helical; Name=VII","evidences":[{"source":"PubMed","id":"27605664","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI11 |
| Number of Residues | 56 |
| Details | Transmembrane: {"description":"Helical; Name=VIII","evidences":[{"source":"PubMed","id":"27605664","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI12 |
| Number of Residues | 240 |
| Details | Topological domain: {"description":"Mitochondrial matrix","evidences":[{"source":"PubMed","id":"27605664","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI13 |
| Number of Residues | 42 |
| Details | Transmembrane: {"description":"Helical; Name=IX","evidences":[{"source":"PubMed","id":"27605664","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI14 |
| Number of Residues | 558 |
| Details | Topological domain: {"description":"Mitochondrial intermembrane","evidences":[{"source":"PubMed","id":"27605664","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI15 |
| Number of Residues | 58 |
| Details | Transmembrane: {"description":"Helical; Name=X","evidences":[{"source":"PubMed","id":"27605664","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI16 |
| Number of Residues | 52 |
| Details | Transmembrane: {"description":"Helical; Name=XI","evidences":[{"source":"PubMed","id":"27605664","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI17 |
| Number of Residues | 62 |
| Details | Transmembrane: {"description":"Helical; Name=XII","evidences":[{"source":"PubMed","id":"27605664","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI18 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"27605664","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23537388","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI19 |
| Number of Residues | 6 |
| Details | Binding site: {"description":"axial binding residue","evidences":[{"source":"PubMed","id":"20385840","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8638158","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI20 |
| Number of Residues | 22 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"20385840","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8638158","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI21 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI22 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N-formylmethionine","evidences":[{"source":"PubMed","id":"2165784","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI23 |
| Number of Residues | 4 |
| Details | Cross-link: {"description":"1'-histidyl-3'-tyrosine (His-Tyr)","evidences":[{"source":"PubMed","id":"10338009","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI24 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N-formylmethionine","evidences":[{"source":"PubMed","id":"220175","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI25 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P00406","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI26 |
| Number of Residues | 384 |
| Details | Transmembrane: {"description":"Helical","evidences":[{"source":"PubMed","id":"27605664","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI27 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P19783","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI28 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P13073","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI29 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P10888","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI30 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P19783","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI31 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P12787","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI32 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P20674","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI33 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"20385840","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"27605664","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8638158","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI34 |
| Number of Residues | 6 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P19536","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI35 |
| Number of Residues | 92 |
| Details | Domain: {"description":"CHCH","evidences":[{"source":"PROSITE-ProRule","id":"PRU01150","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI36 |
| Number of Residues | 20 |
| Details | Motif: {"description":"Cx9C motif","evidences":[{"source":"PROSITE-ProRule","id":"PRU01150","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI37 |
| Number of Residues | 22 |
| Details | Motif: {"description":"Cx10C motif","evidences":[{"source":"PROSITE-ProRule","id":"PRU01150","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI38 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P56391","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI39 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P17665","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 7 |
| Details | Annotated By Reference To The Literature 1ar1 |
| Chain | Residue | Details |
| N | ARG438 | |
| N | PHE377 | |
| N | ARG439 | |
| N | HIS376 | |
| N | HIS240 | |
| N | TYR244 | |
| N | HIS378 |
| site_id | CSA2 |
| Number of Residues | 7 |
| Details | Annotated By Reference To The Literature 1ar1 |
| Chain | Residue | Details |
| A | ARG438 | |
| A | PHE377 | |
| A | ARG439 | |
| A | HIS376 | |
| A | HIS240 | |
| A | TYR244 | |
| A | HIS378 |
| site_id | CSA3 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ar1 |
| Chain | Residue | Details |
| A | GLU242 | |
| A | LYS319 |
| site_id | CSA4 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ar1 |
| Chain | Residue | Details |
| N | GLU242 | |
| N | LYS319 |
| site_id | MCSA1 |
| Number of Residues | 14 |
| Details | M-CSA 124 |
| Chain | Residue | Details |
| A | HIS61 | metal ligand |
| A | HIS290 | metal ligand |
| A | HIS291 | metal ligand, proton acceptor, proton donor |
| A | THR316 | proton acceptor, proton donor, proton relay |
| A | LYS319 | proton acceptor, proton donor, proton relay |
| A | ARG438 | proton acceptor, proton donor, proton relay |
| A | ASP91 | proton acceptor, proton donor, proton relay |
| A | TRP126 | proton acceptor, proton donor, proton relay |
| A | SER156 | proton acceptor, proton donor, proton relay |
| A | SER157 | proton acceptor, proton donor, proton relay |
| A | HIS240 | covalently attached, electrostatic stabiliser, metal ligand, radical stabiliser |
| A | GLU242 | proton acceptor, proton donor, proton relay |
| A | TYR244 | covalently attached, hydrogen radical donor, proton acceptor, proton donor, proton relay, single electron acceptor |
| A | SER255 | proton acceptor, proton donor, proton relay |
| site_id | MCSA2 |
| Number of Residues | 14 |
| Details | M-CSA 124 |
| Chain | Residue | Details |
| N | HIS61 | metal ligand |
| N | HIS290 | metal ligand |
| N | HIS291 | metal ligand, proton acceptor, proton donor |
| N | THR316 | proton acceptor, proton donor, proton relay |
| N | LYS319 | proton acceptor, proton donor, proton relay |
| N | ARG438 | proton acceptor, proton donor, proton relay |
| N | ASP91 | proton acceptor, proton donor, proton relay |
| N | TRP126 | proton acceptor, proton donor, proton relay |
| N | SER156 | proton acceptor, proton donor, proton relay |
| N | SER157 | proton acceptor, proton donor, proton relay |
| N | HIS240 | covalently attached, electrostatic stabiliser, metal ligand, radical stabiliser |
| N | GLU242 | proton acceptor, proton donor, proton relay |
| N | TYR244 | covalently attached, hydrogen radical donor, proton acceptor, proton donor, proton relay, single electron acceptor |
| N | SER255 | proton acceptor, proton donor, proton relay |
