3AXK
Structure of rice Rubisco in complex with NADP(H)
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0004497 | molecular_function | monooxygenase activity |
| A | 0009507 | cellular_component | chloroplast |
| A | 0009536 | cellular_component | plastid |
| 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 | 0046872 | molecular_function | metal ion binding |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0000287 | molecular_function | magnesium ion binding |
| B | 0004497 | molecular_function | monooxygenase activity |
| B | 0009507 | cellular_component | chloroplast |
| B | 0009536 | cellular_component | plastid |
| 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 | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE GOL A 501 |
| Chain | Residue |
| A | LEU270 |
| A | GLY273 |
| A | MET297 |
| A | ILE301 |
| A | HOH627 |
| A | HOH628 |
| A | HOH629 |
| B | LEU270 |
| B | ILE301 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL A 502 |
| Chain | Residue |
| A | HIS86 |
| A | GLU88 |
| A | LYS356 |
| A | ARG358 |
| B | HOH976 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG A 478 |
| Chain | Residue |
| A | KCX201 |
| A | ASP203 |
| A | GLU204 |
| A | HOH616 |
| A | HOH693 |
| A | HOH901 |
| site_id | AC4 |
| Number of Residues | 28 |
| Details | BINDING SITE FOR RESIDUE NDP A 479 |
| Chain | Residue |
| A | LYS175 |
| A | HIS294 |
| A | ARG295 |
| A | HIS298 |
| A | SER379 |
| A | GLY380 |
| A | GLY381 |
| A | GLY403 |
| A | GLY404 |
| A | GLY405 |
| A | HOH580 |
| A | HOH595 |
| A | HOH614 |
| A | HOH616 |
| A | HOH693 |
| A | HOH758 |
| A | HOH1073 |
| A | HOH1080 |
| A | HOH1081 |
| A | HOH1083 |
| A | HOH1085 |
| A | HOH1086 |
| A | HOH1115 |
| B | GLU60 |
| B | ASN123 |
| B | GLY126 |
| B | PHE127 |
| B | HOH733 |
| site_id | AC5 |
| Number of Residues | 32 |
| Details | BINDING SITE FOR RESIDUE NDP A 480 |
| Chain | Residue |
| A | GLU60 |
| A | THR68 |
| A | ASN123 |
| A | GLY126 |
| A | PHE127 |
| A | HOH534 |
| A | HOH594 |
| A | HOH854 |
| A | HOH1074 |
| A | HOH1076 |
| A | HOH1090 |
| A | HOH1091 |
| A | HOH1092 |
| A | HOH1093 |
| A | HOH1096 |
| B | LYS175 |
| B | HIS294 |
| B | ARG295 |
| B | HIS298 |
| B | SER379 |
| B | GLY380 |
| B | GLY381 |
| B | ILE382 |
| B | GLY404 |
| B | GLY405 |
| B | HOH696 |
| B | HOH787 |
| B | HOH855 |
| B | HOH1078 |
| B | HOH1079 |
| B | HOH1087 |
| B | HOH1125 |
| site_id | AC6 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE GOL B 503 |
| Chain | Residue |
| A | SER145 |
| A | LYS146 |
| A | PHE148 |
| A | ARG213 |
| A | HOH497 |
| A | HOH539 |
| A | HOH1109 |
| B | GLU110 |
| B | GOL504 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL B 504 |
| Chain | Residue |
| A | LYS146 |
| A | THR147 |
| A | HOH894 |
| A | HOH895 |
| B | GOL503 |
| B | HOH654 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG B 478 |
| Chain | Residue |
| B | HOH787 |
| B | HOH855 |
| B | KCX201 |
| B | ASP203 |
| B | GLU204 |
| B | HOH734 |
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 | GLY196-GLU204 |
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_01338","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 15 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"22609438","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3AXK","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Binding site: {"description":"in homodimeric partner","evidences":[{"source":"PubMed","id":"22609438","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1WDD","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3AXM","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 13 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"22609438","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1WDD","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Binding site: {"description":"via carbamate group","evidences":[{"source":"PubMed","id":"22609438","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1WDD","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3AXK","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3AXM","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"22609438","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1WDD","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3AXK","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3AXM","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PDB","id":"1WDD","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"22609438","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 2 |
| Details | Site: {"description":"Transition state stabilizer"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-carboxylysine","evidences":[{"source":"PubMed","id":"22609438","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI11 |
| Number of Residues | 8 |
| Details | Region: {"description":"Interaction with large subunit"} |
| Chain | Residue | Details |
