8IOJ
The Rubisco assembly intermidiate of Rubisco large subunit (RbcL) and Arabidopsis thaliana Rubisco accumulation factor 1 (AtRaf1)
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 | 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 | 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 |
| C | 0000287 | molecular_function | magnesium ion binding |
| C | 0004497 | molecular_function | monooxygenase activity |
| C | 0005515 | molecular_function | protein binding |
| C | 0009853 | biological_process | photorespiration |
| C | 0015977 | biological_process | carbon fixation |
| C | 0015979 | biological_process | photosynthesis |
| C | 0016829 | molecular_function | lyase activity |
| C | 0016984 | molecular_function | ribulose-bisphosphate carboxylase activity |
| C | 0019253 | biological_process | reductive pentose-phosphate cycle |
| C | 0031470 | cellular_component | carboxysome |
| C | 0046872 | molecular_function | metal ion binding |
| D | 0000287 | molecular_function | magnesium ion binding |
| D | 0004497 | molecular_function | monooxygenase activity |
| D | 0005515 | molecular_function | protein binding |
| D | 0009853 | biological_process | photorespiration |
| D | 0015977 | biological_process | carbon fixation |
| D | 0015979 | biological_process | photosynthesis |
| D | 0016829 | molecular_function | lyase activity |
| D | 0016984 | molecular_function | ribulose-bisphosphate carboxylase activity |
| D | 0019253 | biological_process | reductive pentose-phosphate cycle |
| D | 0031470 | cellular_component | carboxysome |
| D | 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 | 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 | 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 | 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 | 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
| site_id | PS00012 |
| Number of Residues | 16 |
| Details | PHOSPHOPANTETHEINE Phosphopantetheine attachment site. LTGISSIEQNRLIVGA |
| Chain | Residue | Details |
| E | LEU121-ALA136 |
| 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 | 16 |
| Details | ACT_SITE: Proton acceptor |
| Chain | Residue | Details |
| A | LYS172 | |
| A | HIS291 | |
| B | LYS172 | |
| B | HIS291 | |
| C | LYS172 | |
| C | HIS291 | |
| D | LYS172 | |
| D | HIS291 | |
| H | LYS172 | |
| H | HIS291 | |
| I | LYS172 | |
| I | HIS291 | |
| J | LYS172 | |
| J | HIS291 | |
| K | LYS172 | |
| K | HIS291 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | BINDING: in homodimeric partner |
| Chain | Residue | Details |
| A | ASN120 | |
| B | ASN120 | |
| C | ASN120 | |
| D | ASN120 | |
| H | ASN120 | |
| I | ASN120 | |
| J | ASN120 | |
| K | ASN120 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 40 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | THR170 | |
| A | LYS174 | |
| A | ARG292 | |
| A | HIS324 | |
| A | SER376 | |
| B | THR170 | |
| B | LYS174 | |
| B | ARG292 | |
| B | HIS324 | |
| B | SER376 | |
| C | THR170 | |
| C | LYS174 | |
| C | ARG292 | |
| C | HIS324 | |
| C | SER376 | |
| D | THR170 | |
| D | LYS174 | |
| D | ARG292 | |
| D | HIS324 | |
| D | SER376 | |
| H | THR170 | |
| H | LYS174 | |
| H | ARG292 | |
| H | HIS324 | |
| H | SER376 | |
| I | THR170 | |
| I | LYS174 | |
| I | ARG292 | |
| I | HIS324 | |
| I | SER376 | |
| J | THR170 | |
| J | LYS174 | |
| J | ARG292 | |
| J | HIS324 | |
| J | SER376 | |
| K | THR170 | |
| K | LYS174 | |
| K | ARG292 | |
| K | HIS324 | |
| K | SER376 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 8 |
| Details | BINDING: via carbamate group => ECO:0000269|PubMed:8245022 |
| Chain | Residue | Details |
| A | LYS198 | |
| B | LYS198 | |
| C | LYS198 | |
| D | LYS198 | |
| H | LYS198 | |
| I | LYS198 | |
| J | LYS198 | |
| K | LYS198 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 16 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:8245022 |
| Chain | Residue | Details |
| A | ASP200 | |
| A | GLU201 | |
| B | ASP200 | |
| B | GLU201 | |
| C | ASP200 | |
| C | GLU201 | |
| D | ASP200 | |
| D | GLU201 | |
| H | ASP200 | |
| H | GLU201 | |
| I | ASP200 | |
| I | GLU201 | |
| J | ASP200 | |
| J | GLU201 | |
| K | ASP200 | |
| K | GLU201 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 8 |
| Details | SITE: Transition state stabilizer |
| Chain | Residue | Details |
| A | LYS331 | |
| B | LYS331 | |
| C | LYS331 | |
| D | LYS331 | |
| H | LYS331 | |
| I | LYS331 | |
| J | LYS331 | |
| K | LYS331 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 8 |
| Details | MOD_RES: N6-carboxylysine => ECO:0000269|PubMed:16593333 |
| Chain | Residue | Details |
| A | LYS198 | |
| B | LYS198 | |
| C | LYS198 | |
| D | LYS198 | |
| H | LYS198 | |
| I | LYS198 | |
| J | LYS198 | |
| K | LYS198 |
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 |
| C | LYS172 | electrostatic stabiliser, metal ligand, proton donor |
| C | LYS198 | metal ligand, nucleophile, proton donor |
| C | ASP200 | metal ligand |
| C | GLU201 | metal ligand |
| C | HIS291 | proton acceptor |
| C | LYS331 | electrostatic stabiliser |
| site_id | MCSA4 |
| Number of Residues | 6 |
| Details | M-CSA 907 |
| Chain | Residue | Details |
| D | LYS172 | electrostatic stabiliser, metal ligand, proton donor |
| D | LYS198 | metal ligand, nucleophile, proton donor |
| D | ASP200 | metal ligand |
| D | GLU201 | metal ligand |
| D | HIS291 | proton acceptor |
| D | 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 |
