1AUS
ACTIVATED UNLIGANDED SPINACH RUBISCO
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| L | 0000287 | molecular_function | magnesium ion binding |
| L | 0004497 | molecular_function | monooxygenase activity |
| L | 0009507 | cellular_component | chloroplast |
| L | 0009536 | cellular_component | plastid |
| 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 |
| M | 0000287 | molecular_function | magnesium ion binding |
| M | 0004497 | molecular_function | monooxygenase activity |
| M | 0009507 | cellular_component | chloroplast |
| M | 0009536 | cellular_component | plastid |
| M | 0009853 | biological_process | photorespiration |
| M | 0015977 | biological_process | carbon fixation |
| M | 0015979 | biological_process | photosynthesis |
| M | 0016491 | molecular_function | oxidoreductase activity |
| M | 0016829 | molecular_function | lyase activity |
| M | 0016984 | molecular_function | ribulose-bisphosphate carboxylase activity |
| M | 0019253 | biological_process | reductive pentose-phosphate cycle |
| M | 0046872 | molecular_function | metal ion binding |
| N | 0000287 | molecular_function | magnesium ion binding |
| N | 0004497 | molecular_function | monooxygenase activity |
| N | 0009507 | cellular_component | chloroplast |
| N | 0009536 | cellular_component | plastid |
| N | 0009853 | biological_process | photorespiration |
| N | 0015977 | biological_process | carbon fixation |
| N | 0015979 | biological_process | photosynthesis |
| N | 0016491 | molecular_function | oxidoreductase activity |
| N | 0016829 | molecular_function | lyase activity |
| N | 0016984 | molecular_function | ribulose-bisphosphate carboxylase activity |
| N | 0019253 | biological_process | reductive pentose-phosphate cycle |
| N | 0046872 | molecular_function | metal ion binding |
| O | 0000287 | molecular_function | magnesium ion binding |
| O | 0004497 | molecular_function | monooxygenase activity |
| O | 0009507 | cellular_component | chloroplast |
| O | 0009536 | cellular_component | plastid |
| O | 0009853 | biological_process | photorespiration |
| O | 0015977 | biological_process | carbon fixation |
| O | 0015979 | biological_process | photosynthesis |
| O | 0016491 | molecular_function | oxidoreductase activity |
| O | 0016829 | molecular_function | lyase activity |
| O | 0016984 | molecular_function | ribulose-bisphosphate carboxylase activity |
| O | 0019253 | biological_process | reductive pentose-phosphate cycle |
| O | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG L 476 |
| Chain | Residue |
| L | ASP203 |
| L | GLU204 |
| L | FMT477 |
| L | HOH570 |
| L | HOH588 |
| L | HOH623 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details |
| Chain | Residue |
| L | LYS201 |
| L | ASP203 |
| L | GLU204 |
| M | MG476 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details |
| Chain | Residue |
| L | ASP203 |
| L | GLU204 |
| N | MG476 |
| L | LYS201 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details |
| Chain | Residue |
| L | LYS201 |
| L | ASP203 |
| L | GLU204 |
| O | MG476 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MG M 476 |
| Chain | Residue |
| M | ASP203 |
| M | GLU204 |
| M | FMT477 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MG N 476 |
| Chain | Residue |
| N | ASP203 |
| N | GLU204 |
| N | FMT477 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MG O 476 |
| Chain | Residue |
| O | ASP203 |
| O | GLU204 |
| O | FMT477 |
| site_id | AC8 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE FMT L 477 |
| Chain | Residue |
| L | THR173 |
| L | LYS201 |
| L | ASP203 |
| L | GLU204 |
| L | HIS294 |
| L | HIS327 |
| L | MG476 |
| L | HOH588 |
| L | HOH653 |
| site_id | AC9 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE FMT M 477 |
| Chain | Residue |
| M | THR173 |
| M | LYS201 |
| M | ASP203 |
| M | GLU204 |
| M | HIS294 |
| M | HIS327 |
| M | MG476 |
| site_id | ACT |
| Number of Residues | 4 |
| Details | CATALYTIC RESIDUES |
| Chain | Residue |
| L | LYS201 |
| L | ASP203 |
| L | GLU204 |
| L | MG476 |
| site_id | AD1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE FMT N 477 |
| Chain | Residue |
| N | THR173 |
| N | LYS201 |
| N | ASP203 |
| N | GLU204 |
| N | HIS294 |
| N | HIS327 |
| N | MG476 |
| site_id | AD2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE FMT O 477 |
| Chain | Residue |
| O | THR173 |
| O | LYS201 |
| O | ASP203 |
| O | GLU204 |
| O | HIS294 |
| O | HIS327 |
| O | MG476 |
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 | 16 |
| 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 | 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 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 6 |
| Details | Annotated By Reference To The Literature 1rbl |
| Chain | Residue | Details |
| L | LYS175 | |
| L | LYS201 | |
| L | LYS177 | |
| L | HIS294 | |
| L | ASP203 | |
| L | HIS327 |
| site_id | CSA2 |
| Number of Residues | 6 |
| Details | Annotated By Reference To The Literature 1rbl |
| Chain | Residue | Details |
| M | LYS175 | |
| M | LYS201 | |
| M | LYS177 | |
| M | HIS294 | |
| M | ASP203 | |
| M | HIS327 |
| site_id | CSA3 |
| Number of Residues | 6 |
| Details | Annotated By Reference To The Literature 1rbl |
| Chain | Residue | Details |
| N | LYS175 | |
| N | LYS201 | |
| N | LYS177 | |
| N | HIS294 | |
| N | ASP203 | |
| N | HIS327 |
| site_id | CSA4 |
| Number of Residues | 6 |
| Details | Annotated By Reference To The Literature 1rbl |
| Chain | Residue | Details |
| O | LYS175 | |
| O | LYS201 | |
| O | LYS177 | |
| O | HIS294 | |
| O | ASP203 | |
| O | HIS327 |
