8ILM
The cryo-EM structure of eight Rubisco large subunits (RbcL), two Arabidopsis thaliana Rubisco accumulation factors 1 (AtRaf1), and seven Arabidopsis thaliana Bundle Sheath Defective 2 (AtBSD2)
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0004497 | molecular_function | monooxygenase activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0009853 | biological_process | photorespiration |
| 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 | 0031470 | cellular_component | carboxysome |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0000287 | molecular_function | magnesium ion binding |
| B | 0004497 | molecular_function | monooxygenase activity |
| B | 0005515 | molecular_function | protein binding |
| 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 | 0031470 | cellular_component | carboxysome |
| B | 0046872 | molecular_function | metal ion binding |
| F | 0000287 | molecular_function | magnesium ion binding |
| F | 0004497 | molecular_function | monooxygenase activity |
| F | 0005515 | molecular_function | protein binding |
| F | 0009853 | biological_process | photorespiration |
| F | 0015977 | biological_process | carbon fixation |
| F | 0015979 | biological_process | photosynthesis |
| F | 0016491 | molecular_function | oxidoreductase activity |
| F | 0016829 | molecular_function | lyase activity |
| F | 0016984 | molecular_function | ribulose-bisphosphate carboxylase activity |
| F | 0019253 | biological_process | reductive pentose-phosphate cycle |
| F | 0031470 | cellular_component | carboxysome |
| F | 0046872 | molecular_function | metal ion binding |
| G | 0000287 | molecular_function | magnesium ion binding |
| G | 0004497 | molecular_function | monooxygenase activity |
| G | 0005515 | molecular_function | protein binding |
| G | 0009853 | biological_process | photorespiration |
| G | 0015977 | biological_process | carbon fixation |
| G | 0015979 | biological_process | photosynthesis |
| G | 0016491 | molecular_function | oxidoreductase activity |
| G | 0016829 | molecular_function | lyase activity |
| G | 0016984 | molecular_function | ribulose-bisphosphate carboxylase activity |
| G | 0019253 | biological_process | reductive pentose-phosphate cycle |
| G | 0031470 | cellular_component | carboxysome |
| G | 0046872 | molecular_function | metal ion binding |
| H | 0000287 | molecular_function | magnesium ion binding |
| H | 0004497 | molecular_function | monooxygenase activity |
| H | 0005515 | molecular_function | protein binding |
| 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 | 0031470 | cellular_component | carboxysome |
| H | 0046872 | molecular_function | metal ion binding |
| I | 0000287 | molecular_function | magnesium ion binding |
| I | 0004497 | molecular_function | monooxygenase activity |
| I | 0005515 | molecular_function | protein binding |
| I | 0009853 | biological_process | photorespiration |
| I | 0015977 | biological_process | carbon fixation |
| I | 0015979 | biological_process | photosynthesis |
| I | 0016491 | molecular_function | oxidoreductase activity |
| I | 0016829 | molecular_function | lyase activity |
| I | 0016984 | molecular_function | ribulose-bisphosphate carboxylase activity |
| I | 0019253 | biological_process | reductive pentose-phosphate cycle |
| I | 0031470 | cellular_component | carboxysome |
| I | 0046872 | molecular_function | metal ion binding |
| J | 0000287 | molecular_function | magnesium ion binding |
| J | 0004497 | molecular_function | monooxygenase activity |
| J | 0005515 | molecular_function | protein binding |
| J | 0009853 | biological_process | photorespiration |
| J | 0015977 | biological_process | carbon fixation |
| J | 0015979 | biological_process | photosynthesis |
| J | 0016491 | molecular_function | oxidoreductase activity |
| J | 0016829 | molecular_function | lyase activity |
| J | 0016984 | molecular_function | ribulose-bisphosphate carboxylase activity |
| J | 0019253 | biological_process | reductive pentose-phosphate cycle |
| J | 0031470 | cellular_component | carboxysome |
| J | 0046872 | molecular_function | metal ion binding |
| K | 0000287 | molecular_function | magnesium ion binding |
| K | 0004497 | molecular_function | monooxygenase activity |
| K | 0005515 | molecular_function | protein binding |
| K | 0009853 | biological_process | photorespiration |
| K | 0015977 | biological_process | carbon fixation |
| K | 0015979 | biological_process | photosynthesis |
| K | 0016491 | molecular_function | oxidoreductase activity |
| K | 0016829 | molecular_function | lyase activity |
| K | 0016984 | molecular_function | ribulose-bisphosphate carboxylase activity |
| K | 0019253 | biological_process | reductive pentose-phosphate cycle |
| K | 0031470 | cellular_component | carboxysome |
| K | 0046872 | molecular_function | metal ion binding |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 24 |
| 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 | 16 |
| Details | Active site: {"description":"Proton acceptor"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 8 |
| Details | Binding site: {"description":"in homodimeric partner"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 40 |
| Details | Binding site: {} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 8 |
| 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 | 16 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"8245022","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 8 |
| Details | Site: {"description":"Transition state stabilizer"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 8 |
| Details | Modified residue: {"description":"N6-carboxylysine","evidences":[{"source":"PubMed","id":"16593333","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 355 |
| Details | Zinc finger: {"description":"CR-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU00546","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 56 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"29217567","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6EKB","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6EKC","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI11 |
| Number of Residues | 21 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"29217567","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6EKB","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI12 |
| Number of Residues | 378 |
| Details | Region: {"description":"N-terminal alpha-helix","evidences":[{"source":"PubMed","id":"26237510","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI13 |
| Number of Residues | 146 |
| Details | Region: {"description":"C-terminal beta sheet","evidences":[{"source":"PubMed","id":"26237510","evidenceCode":"ECO:0000305"}]} |
| 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 |
| B | LYS172 | electrostatic stabiliser, metal ligand, proton donor |
| B | LYS198 | metal ligand, nucleophile, proton donor |
| B | ASP200 | metal ligand |
| B | GLU201 | metal ligand |
| B | HIS291 | proton acceptor |
| B | LYS331 | electrostatic stabiliser |
| site_id | MCSA3 |
| Number of Residues | 6 |
| Details | M-CSA 907 |
| Chain | Residue | Details |
| F | LYS172 | electrostatic stabiliser, metal ligand, proton donor |
| F | LYS198 | metal ligand, nucleophile, proton donor |
| F | ASP200 | metal ligand |
| F | GLU201 | metal ligand |
| F | HIS291 | proton acceptor |
| F | LYS331 | electrostatic stabiliser |
| site_id | MCSA4 |
| Number of Residues | 6 |
| Details | M-CSA 907 |
| Chain | Residue | Details |
| G | LYS172 | electrostatic stabiliser, metal ligand, proton donor |
| G | LYS198 | metal ligand, nucleophile, proton donor |
| G | ASP200 | metal ligand |
| G | GLU201 | metal ligand |
| G | HIS291 | proton acceptor |
| G | LYS331 | electrostatic stabiliser |
| site_id | MCSA5 |
| Number of Residues | 6 |
| Details | M-CSA 907 |
| Chain | Residue | Details |
| H | LYS172 | electrostatic stabiliser, metal ligand, proton donor |
| H | LYS198 | metal ligand, nucleophile, proton donor |
| H | ASP200 | metal ligand |
| H | GLU201 | metal ligand |
| H | HIS291 | proton acceptor |
| H | LYS331 | electrostatic stabiliser |
| site_id | MCSA6 |
| Number of Residues | 6 |
| Details | M-CSA 907 |
| Chain | Residue | Details |
| I | LYS172 | electrostatic stabiliser, metal ligand, proton donor |
| I | LYS198 | metal ligand, nucleophile, proton donor |
| I | ASP200 | metal ligand |
| I | GLU201 | metal ligand |
| I | HIS291 | proton acceptor |
| I | LYS331 | electrostatic stabiliser |
| site_id | MCSA7 |
| Number of Residues | 6 |
| Details | M-CSA 907 |
| Chain | Residue | Details |
| J | LYS172 | electrostatic stabiliser, metal ligand, proton donor |
| J | LYS198 | metal ligand, nucleophile, proton donor |
| J | ASP200 | metal ligand |
| J | GLU201 | metal ligand |
| J | HIS291 | proton acceptor |
| J | LYS331 | electrostatic stabiliser |
| site_id | MCSA8 |
| Number of Residues | 6 |
| Details | M-CSA 907 |
| Chain | Residue | Details |
| K | LYS172 | electrostatic stabiliser, metal ligand, proton donor |
| K | LYS198 | metal ligand, nucleophile, proton donor |
| K | ASP200 | metal ligand |
| K | GLU201 | metal ligand |
| K | HIS291 | proton acceptor |
| K | LYS331 | electrostatic stabiliser |
