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 | 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 | 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 | 10 |
| Details | BINDING SITE FOR RESIDUE RUB A 600 |
| Chain | Residue |
| A | ILE164 |
| A | ASP193 |
| A | HIS321 |
| A | ILE366 |
| A | SER368 |
| A | ALA392 |
| A | GLY393 |
| A | MG500 |
| A | FMT601 |
| B | ASN111 |
| site_id | AC2 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE RUB B 700 |
| Chain | Residue |
| B | ILE164 |
| B | HIS287 |
| B | HIS321 |
| B | THR322 |
| B | SER368 |
| B | GLY369 |
| B | THR391 |
| B | ALA392 |
| B | GLY393 |
| B | MG500 |
| B | FMT701 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MG A 500 |
| Chain | Residue |
| A | ASP193 |
| A | RUB600 |
| A | FMT601 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG B 500 |
| Chain | Residue |
| B | ASP193 |
| B | GLU194 |
| B | RUB700 |
| B | FMT701 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE FMT A 601 |
| Chain | Residue |
| A | ILE164 |
| A | LYS191 |
| A | ASN192 |
| A | ASP193 |
| A | MG500 |
| A | RUB600 |
| site_id | AC6 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE FMT B 701 |
| Chain | Residue |
| B | LYS191 |
| B | ASP193 |
| B | GLU194 |
| B | HIS287 |
| B | HIS321 |
| B | MG500 |
| B | RUB700 |
| site_id | ACT |
| Number of Residues | 5 |
| Details | ACTIVE SITE CHAIN A |
| Chain | Residue |
| A | FMT601 |
| A | LYS191 |
| A | ASP193 |
| A | GLU194 |
| A | MG500 |
| site_id | BCT |
| Number of Residues | 5 |
| Details | ACTIVE SITE CHAIN B |
| Chain | Residue |
| B | MG500 |
| B | FMT701 |
| B | LYS191 |
| B | ASP193 |
| B | GLU194 |
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 | GLY186-GLU194 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | ACT_SITE: Proton acceptor |
| Chain | Residue | Details |
| A | LYS166 | |
| A | HIS287 | |
| B | LYS166 | |
| B | HIS287 | |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | BINDING: in homodimeric partner |
| Chain | Residue | Details |
| A | ASN111 | |
| B | ASN111 | |
| site_id | SWS_FT_FI3 |
| Number of Residues | 8 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | LYS168 | |
| A | ARG288 | |
| A | HIS321 | |
| A | SER368 | |
| B | LYS168 | |
| B | ARG288 | |
| B | HIS321 | |
| B | SER368 | |
| Chain | Residue | Details |
| A | LYS191 | |
| B | LYS191 | |
| Chain | Residue | Details |
| A | ASP193 | |
| A | GLU194 | |
| B | ASP193 | |
| B | GLU194 | |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | SITE: Transition state stabilizer |
| Chain | Residue | Details |
| A | LYS329 | |
| B | LYS329 | |
| Chain | Residue | Details |
| A | LYS191 | |
| B | LYS191 | |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 5 |
| Details | Annotated By Reference To The Literature 1rbl |
| Chain | Residue | Details |
| A | ASN192 | |
| A | HIS287 | |
| A | LYS166 | |
| A | LYS191 | |
| A | HIS321 | |
| site_id | CSA2 |
| Number of Residues | 5 |
| Details | Annotated By Reference To The Literature 1rbl |
| Chain | Residue | Details |
| B | ASN192 | |
| B | HIS287 | |
| B | LYS166 | |
| B | LYS191 | |
| B | HIS321 | |
| site_id | CSA3 |
| Number of Residues | 6 |
| Details | Annotated By Reference To The Literature 1rbl |
| Chain | Residue | Details |
| A | HIS287 | |
| A | LYS166 | |
| A | ASP193 | |
| A | LYS191 | |
| A | HIS321 | |
| A | LYS168 | |
| site_id | CSA4 |
| Number of Residues | 6 |
| Details | Annotated By Reference To The Literature 1rbl |
| Chain | Residue | Details |
| B | HIS287 | |
| B | LYS166 | |
| B | ASP193 | |
| B | LYS191 | |
| B | HIS321 | |
| B | LYS168 | |
| site_id | MCSA1 |
| Number of Residues | 8 |
| Details | M-CSA 797 |
| Chain | Residue | Details |
| A | LYS166 | electrostatic stabiliser, proton acceptor, proton donor |
| A | LYS191 | electron pair donor, metal ligand, nucleophile |
| A | ASN192 | electrostatic stabiliser |
| A | ASP193 | metal ligand |
| A | GLU194 | metal ligand |
| A | HIS287 | activator, increase nucleophilicity, proton acceptor |
| A | HIS321 | electrostatic stabiliser |
| A | LYS329 | electrostatic stabiliser |
| site_id | MCSA2 |
| Number of Residues | 8 |
| Details | M-CSA 797 |
| Chain | Residue | Details |
| B | LYS166 | electrostatic stabiliser, proton acceptor, proton donor |
| B | LYS191 | electron pair donor, metal ligand, nucleophile |
| B | ASN192 | electrostatic stabiliser |
| B | ASP193 | metal ligand |
| B | GLU194 | metal ligand |
| B | HIS287 | activator, increase nucleophilicity, proton acceptor |
| B | HIS321 | electrostatic stabiliser |
| B | LYS329 | electrostatic stabiliser |
