Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0004497 | molecular_function | monooxygenase activity |
| A | 0015977 | biological_process | carbon fixation |
| A | 0015979 | biological_process | photosynthesis |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016829 | molecular_function | lyase activity |
| A | 0016984 | molecular_function | ribulose-bisphosphate carboxylase activity |
| A | 0019253 | biological_process | reductive pentose-phosphate cycle |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0000287 | molecular_function | magnesium ion binding |
| B | 0004497 | molecular_function | monooxygenase activity |
| 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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 28 |
| Details | binding site for residue CAP A 501 |
| Chain | Residue |
| A | ILE165 |
| A | LYS330 |
| A | MET331 |
| A | SER369 |
| A | GLY370 |
| A | GLY371 |
| A | GLY394 |
| A | GLY395 |
| A | MG502 |
| A | HOH614 |
| A | HOH617 |
| A | LYS167 |
| A | HOH644 |
| A | HOH666 |
| A | HOH681 |
| A | HOH687 |
| A | HOH688 |
| B | GLU49 |
| B | THR54 |
| B | ASN112 |
| B | HOH626 |
| A | LYS169 |
| A | KCX192 |
| A | ASP194 |
| A | GLU195 |
| A | HIS288 |
| A | ARG289 |
| A | HIS322 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | binding site for residue MG A 502 |
| Chain | Residue |
| A | LYS169 |
| A | KCX192 |
| A | ASP194 |
| A | GLU195 |
| A | CAP501 |
| B | ASN112 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | binding site for residue K A 503 |
| Chain | Residue |
| A | LEU10 |
| A | LEU12 |
| A | TYR73 |
| site_id | AC4 |
| Number of Residues | 23 |
| Details | binding site for residue CAP B 501 |
| Chain | Residue |
| A | THR54 |
| A | ASN112 |
| B | ILE165 |
| B | LYS167 |
| B | LYS169 |
| B | KCX192 |
| B | ASP194 |
| B | GLU195 |
| B | HIS288 |
| B | ARG289 |
| B | HIS322 |
| B | LYS330 |
| B | MET331 |
| B | SER369 |
| B | GLY370 |
| B | GLY371 |
| B | GLY394 |
| B | GLY395 |
| B | MG502 |
| B | HOH604 |
| B | HOH615 |
| B | HOH623 |
| B | HOH697 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | binding site for residue MG B 502 |
| Chain | Residue |
| A | ASN112 |
| B | KCX192 |
| B | ASP194 |
| B | GLU195 |
| B | CAP501 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | binding site for residue K B 503 |
| Chain | Residue |
| B | LEU10 |
| B | LEU12 |
| B | TYR73 |
| B | HOH718 |
Functional Information from PROSITE/UniProt
| site_id | PS00157 |
| Number of Residues | 9 |
| Details | RUBISCO_LARGE Ribulose bisphosphate carboxylase large chain active site. GgDFiKnDE |
| Chain | Residue | Details |
| A | GLY187-GLU195 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_01339","evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Binding site: {"description":"in homodimeric partner","evidences":[{"source":"HAMAP-Rule","id":"MF_01339","evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 12 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01339","evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Binding site: {"description":"via carbamate group","evidences":[{"source":"HAMAP-Rule","id":"MF_01339","evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Site: {"description":"Transition state stabilizer","evidences":[{"source":"HAMAP-Rule","id":"MF_01339","evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-carboxylysine","evidences":[{"source":"HAMAP-Rule","id":"MF_01339","evidenceCode":"ECO:0000255"}]} |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 8 |
| Details | M-CSA 797 |
| Chain | Residue | Details |
| A | LYS167 | electrostatic stabiliser, proton acceptor, proton donor |
| A | KCX192 | electron pair donor, metal ligand, nucleophile |
| A | GLN197 | electrostatic stabiliser |
| A | GLY198 | metal ligand |
| A | ASN199 | metal ligand |
| A | HIS292 | activator, increase nucleophilicity, proton acceptor |
| A | MET326 | electrostatic stabiliser |
| A | GLU334 | electrostatic stabiliser |
| site_id | MCSA2 |
| Number of Residues | 8 |
| Details | M-CSA 797 |
| Chain | Residue | Details |
| B | LYS167 | electrostatic stabiliser, proton acceptor, proton donor |
| B | KCX192 | electron pair donor, metal ligand, nucleophile |
| B | GLN197 | electrostatic stabiliser |
| B | GLY198 | metal ligand |
| B | ASN199 | metal ligand |
| B | HIS292 | activator, increase nucleophilicity, proton acceptor |
| B | MET326 | electrostatic stabiliser |
| B | GLU334 | electrostatic stabiliser |
