3RG6
Crystal structure of a chaperone-bound assembly intermediate of form I Rubisco
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0005515 | molecular_function | protein binding |
| A | 0015977 | biological_process | carbon fixation |
| A | 0016984 | molecular_function | ribulose-bisphosphate carboxylase activity |
| A | 0019253 | biological_process | reductive pentose-phosphate cycle |
| A | 0031470 | cellular_component | carboxysome |
| B | 0000287 | molecular_function | magnesium ion binding |
| B | 0005515 | molecular_function | protein binding |
| B | 0015977 | biological_process | carbon fixation |
| B | 0016984 | molecular_function | ribulose-bisphosphate carboxylase activity |
| B | 0019253 | biological_process | reductive pentose-phosphate cycle |
| B | 0031470 | cellular_component | carboxysome |
| C | 0005515 | molecular_function | protein binding |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0006457 | biological_process | protein folding |
| C | 0015977 | biological_process | carbon fixation |
| C | 0031470 | cellular_component | carboxysome |
| C | 0042803 | molecular_function | protein homodimerization activity |
| C | 0044183 | molecular_function | protein folding chaperone |
| C | 0110102 | biological_process | ribulose bisphosphate carboxylase complex assembly |
| D | 0005515 | molecular_function | protein binding |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0006457 | biological_process | protein folding |
| D | 0015977 | biological_process | carbon fixation |
| D | 0031470 | cellular_component | carboxysome |
| D | 0042803 | molecular_function | protein homodimerization activity |
| D | 0044183 | molecular_function | protein folding chaperone |
| D | 0110102 | biological_process | ribulose bisphosphate carboxylase complex assembly |
| E | 0005515 | molecular_function | protein binding |
| E | 0005737 | cellular_component | cytoplasm |
| E | 0006457 | biological_process | protein folding |
| E | 0015977 | biological_process | carbon fixation |
| E | 0031470 | cellular_component | carboxysome |
| E | 0042803 | molecular_function | protein homodimerization activity |
| E | 0044183 | molecular_function | protein folding chaperone |
| E | 0110102 | biological_process | ribulose bisphosphate carboxylase complex assembly |
| F | 0005515 | molecular_function | protein binding |
| F | 0005737 | cellular_component | cytoplasm |
| F | 0006457 | biological_process | protein folding |
| F | 0015977 | biological_process | carbon fixation |
| F | 0031470 | cellular_component | carboxysome |
| F | 0042803 | molecular_function | protein homodimerization activity |
| F | 0044183 | molecular_function | protein folding chaperone |
| F | 0110102 | biological_process | ribulose bisphosphate carboxylase complex assembly |
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 |
| A | GLY193-GLU201 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 12 |
| Details | Motif: {"description":"Interacts with RbcX2","evidences":[{"source":"PubMed","id":"17574029","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | Active site: {"description":"Proton acceptor"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Binding site: {"description":"in homodimeric partner"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 10 |
| Details | Binding site: {} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Binding site: {"description":"via carbamate group","evidences":[{"source":"PubMed","id":"8245022","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"8245022","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | Site: {"description":"Transition state stabilizer"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-carboxylysine","evidences":[{"source":"PubMed","id":"16593333","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 6 |
| Details | M-CSA 907 |
| Chain | Residue | Details |
| A | LYS172 | electrostatic stabiliser, metal ligand, proton donor |
| A | LYS198 | metal ligand, nucleophile, proton donor |
| A | ASP200 | metal ligand |
| A | GLU201 | metal ligand |
| A | HIS291 | proton acceptor |
| A | LYS331 | electrostatic stabiliser |
| site_id | MCSA2 |
| Number of Residues | 6 |
| Details | M-CSA 907 |
| Chain | Residue | Details |
