1RXO
ACTIVATED SPINACH RUBISCO IN COMPLEX WITH ITS SUBSTRATE RIBULOSE-1,5-BISPHOSPHATE AND CALCIUM
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| B | 0000287 | molecular_function | magnesium ion binding |
| B | 0004497 | molecular_function | monooxygenase activity |
| B | 0009507 | cellular_component | chloroplast |
| B | 0009853 | biological_process | photorespiration |
| B | 0015977 | biological_process | carbon fixation |
| B | 0015979 | biological_process | photosynthesis |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0016829 | molecular_function | lyase activity |
| B | 0016984 | molecular_function | ribulose-bisphosphate carboxylase activity |
| B | 0019253 | biological_process | reductive pentose-phosphate cycle |
| B | 0046872 | molecular_function | metal ion binding |
| C | 0009507 | cellular_component | chloroplast |
| C | 0009853 | biological_process | photorespiration |
| C | 0015977 | biological_process | carbon fixation |
| C | 0015979 | biological_process | photosynthesis |
| C | 0016984 | molecular_function | ribulose-bisphosphate carboxylase activity |
| C | 0019253 | biological_process | reductive pentose-phosphate cycle |
| E | 0000287 | molecular_function | magnesium ion binding |
| E | 0004497 | molecular_function | monooxygenase activity |
| E | 0009507 | cellular_component | chloroplast |
| E | 0009853 | biological_process | photorespiration |
| E | 0015977 | biological_process | carbon fixation |
| E | 0015979 | biological_process | photosynthesis |
| E | 0016491 | molecular_function | oxidoreductase activity |
| E | 0016829 | molecular_function | lyase activity |
| E | 0016984 | molecular_function | ribulose-bisphosphate carboxylase activity |
| E | 0019253 | biological_process | reductive pentose-phosphate cycle |
| E | 0046872 | molecular_function | metal ion binding |
| F | 0009507 | cellular_component | chloroplast |
| F | 0009853 | biological_process | photorespiration |
| F | 0015977 | biological_process | carbon fixation |
| F | 0015979 | biological_process | photosynthesis |
| F | 0016984 | molecular_function | ribulose-bisphosphate carboxylase activity |
| F | 0019253 | biological_process | reductive pentose-phosphate cycle |
| H | 0000287 | molecular_function | magnesium ion binding |
| H | 0004497 | molecular_function | monooxygenase activity |
| H | 0009507 | cellular_component | chloroplast |
| H | 0009853 | biological_process | photorespiration |
| H | 0015977 | biological_process | carbon fixation |
| H | 0015979 | biological_process | photosynthesis |
| H | 0016491 | molecular_function | oxidoreductase activity |
| H | 0016829 | molecular_function | lyase activity |
| H | 0016984 | molecular_function | ribulose-bisphosphate carboxylase activity |
| H | 0019253 | biological_process | reductive pentose-phosphate cycle |
| H | 0046872 | molecular_function | metal ion binding |
| I | 0009507 | cellular_component | chloroplast |
| I | 0009853 | biological_process | photorespiration |
| I | 0015977 | biological_process | carbon fixation |
| I | 0015979 | biological_process | photosynthesis |
| I | 0016984 | molecular_function | ribulose-bisphosphate carboxylase activity |
| I | 0019253 | biological_process | reductive pentose-phosphate cycle |
| L | 0000287 | molecular_function | magnesium ion binding |
| L | 0004497 | molecular_function | monooxygenase activity |
| L | 0009507 | cellular_component | chloroplast |
| L | 0009853 | biological_process | photorespiration |
| L | 0015977 | biological_process | carbon fixation |
| L | 0015979 | biological_process | photosynthesis |
| L | 0016491 | molecular_function | oxidoreductase activity |
| L | 0016829 | molecular_function | lyase activity |
| L | 0016984 | molecular_function | ribulose-bisphosphate carboxylase activity |
| L | 0019253 | biological_process | reductive pentose-phosphate cycle |
| L | 0046872 | molecular_function | metal ion binding |
| S | 0009507 | cellular_component | chloroplast |
| S | 0009853 | biological_process | photorespiration |
| S | 0015977 | biological_process | carbon fixation |
| S | 0015979 | biological_process | photosynthesis |
| S | 0016984 | molecular_function | ribulose-bisphosphate carboxylase activity |
| S | 0019253 | biological_process | reductive pentose-phosphate cycle |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE RUB L 476 |
| Chain | Residue |
| E | TRP66 |
| L | LYS175 |
| L | KCX201 |
| L | GLU204 |
| L | HIS294 |
| L | ARG295 |
| L | HIS298 |
| L | SER379 |
| L | GLY380 |
| L | GLY381 |
| L | GLY403 |
| L | GLY404 |
| L | CA477 |
| L | HOH525 |
| L | HOH526 |
| L | HOH541 |
| L | HOH562 |
| L | HOH568 |
| L | HOH593 |
| L | HOH619 |
| L | HOH660 |
| site_id | AC2 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE RUB B 476 |
| Chain | Residue |
| B | TRP66 |
| B | LYS175 |
| B | KCX201 |
| B | GLU204 |
| B | HIS294 |
| B | ARG295 |
| B | HIS298 |
| B | SER379 |
| B | GLY380 |
| B | GLY381 |
| B | GLY403 |
| B | GLY404 |
| B | CA477 |
| B | HOH526 |
| B | HOH527 |
| B | HOH542 |
| B | HOH563 |
| B | HOH569 |
| B | HOH594 |
| B | HOH620 |
| B | HOH661 |
| site_id | AC3 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE RUB E 476 |
| Chain | Residue |
| E | LYS175 |
| E | KCX201 |
| E | GLU204 |
| E | HIS294 |
| E | ARG295 |
| E | HIS298 |
| E | SER379 |
| E | GLY380 |
| E | GLY381 |
| E | GLY403 |
| E | GLY404 |
| E | CA477 |
| E | HOH566 |
| E | HOH567 |
| E | HOH583 |
| E | HOH606 |
| E | HOH613 |
| E | HOH638 |
| E | HOH665 |
| E | HOH709 |
| L | TRP66 |
| site_id | AC4 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE RUB H 476 |
| Chain | Residue |
| H | TRP66 |
| H | LYS175 |
| H | KCX201 |
| H | GLU204 |
| H | HIS294 |
| H | ARG295 |
| H | HIS298 |
| H | SER379 |
| H | GLY380 |
| H | GLY381 |
| H | GLY403 |
| H | GLY404 |
| H | CA477 |
| H | HOH528 |
| H | HOH529 |
| H | HOH544 |
| H | HOH565 |
| H | HOH571 |
| H | HOH596 |
| H | HOH622 |
| H | HOH663 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA L 477 |
| Chain | Residue |
| L | RUB476 |
| L | HOH583 |
| L | KCX201 |
| L | ASP203 |
| L | GLU204 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA B 477 |
| Chain | Residue |
| B | KCX201 |
| B | ASP203 |
| B | GLU204 |
| B | RUB476 |
| B | HOH584 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA E 477 |
| Chain | Residue |
| E | KCX201 |
| E | ASP203 |
| E | GLU204 |
| E | RUB476 |
| E | HOH628 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA H 477 |
| Chain | Residue |
| H | KCX201 |
| H | ASP203 |
| H | GLU204 |
| H | RUB476 |
| H | HOH586 |
| site_id | ACB |
| Number of Residues | 3 |
| Details | ACTIVE SITE. |
| Chain | Residue |
| B | KCX201 |
| B | ASP203 |
| B | GLU204 |
| site_id | ACE |
| Number of Residues | 3 |
| Details | ACTIVE SITE. |
| Chain | Residue |
| E | KCX201 |
| E | ASP203 |
| E | GLU204 |
| site_id | ACH |
| Number of Residues | 3 |
| Details | ACTIVE SITE. |
| Chain | Residue |
| H | KCX201 |
| H | ASP203 |
| H | GLU204 |
| site_id | ACL |
| Number of Residues | 3 |
| Details | ACTIVE SITE. |
| Chain | Residue |
| L | KCX201 |
| L | ASP203 |
| L | GLU204 |
Functional Information from PROSITE/UniProt
| site_id | PS00157 |
| Number of Residues | 9 |
| Details | RUBISCO_LARGE Ribulose bisphosphate carboxylase large chain active site. GlDFtKdDE |
| Chain | Residue | Details |
| L | GLY196-GLU204 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"2118958","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"637859","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9092835","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"637859","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 20 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"9034362","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1RCX","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | Binding site: {"description":"in homodimeric partner","evidences":[{"source":"PubMed","id":"9034362","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1RCX","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 12 |
| Details | Binding site: {} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 4 |
| Details | Binding site: {"description":"via carbamate group","evidences":[{"source":"PubMed","id":"8648644","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9092835","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"14596800","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"2118958","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"9034362","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"8648644","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9092835","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"14596800","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"2118958","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"9034362","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"9034362","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1RXO","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 12 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"9034362","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1RCX","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1RXO","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 4 |
| Details | Site: {"description":"Not N6-methylated","evidences":[{"source":"PubMed","id":"2928307","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI11 |
| Number of Residues | 4 |
| Details | Site: {"description":"Transition state stabilizer","evidences":[{"source":"PubMed","id":"8955130","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI12 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"N6-carboxylysine","evidences":[{"source":"PubMed","id":"14596800","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"2118958","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8648644","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9034362","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9092835","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI13 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"Methionine derivative"} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 5 |
| Details | Annotated By Reference To The Literature 1rbl |
| Chain | Residue | Details |
| L | LYS175 | |
| L | HIS294 | |
| L | LYS177 | |
| L | ASP203 | |
| L | HIS327 |
| site_id | CSA2 |
| Number of Residues | 5 |
| Details | Annotated By Reference To The Literature 1rbl |
| Chain | Residue | Details |
| B | LYS175 | |
| B | HIS294 | |
| B | LYS177 | |
| B | ASP203 | |
| B | HIS327 |
| site_id | CSA3 |
| Number of Residues | 5 |
| Details | Annotated By Reference To The Literature 1rbl |
| Chain | Residue | Details |
| E | LYS175 | |
| E | HIS294 | |
| E | LYS177 | |
| E | ASP203 | |
| E | HIS327 |
| site_id | CSA4 |
| Number of Residues | 5 |
| Details | Annotated By Reference To The Literature 1rbl |
| Chain | Residue | Details |
| H | LYS175 | |
| H | HIS294 | |
| H | LYS177 | |
| H | ASP203 | |
| H | HIS327 |
