1RCO
SPINACH RUBISCO IN COMPLEX WITH THE INHIBITOR D-XYLULOSE-2,2-DIOL-1,5-BISPHOSPHATE
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| B | 0000287 | molecular_function | magnesium ion binding |
| B | 0009507 | cellular_component | chloroplast |
| B | 0015977 | biological_process | carbon fixation |
| B | 0016984 | molecular_function | ribulose-bisphosphate carboxylase activity |
| B | 0019253 | biological_process | reductive pentose-phosphate cycle |
| C | 0009507 | cellular_component | chloroplast |
| C | 0015977 | biological_process | carbon fixation |
| C | 0016984 | molecular_function | ribulose-bisphosphate carboxylase activity |
| C | 0019253 | biological_process | reductive pentose-phosphate cycle |
| E | 0000287 | molecular_function | magnesium ion binding |
| E | 0009507 | cellular_component | chloroplast |
| E | 0015977 | biological_process | carbon fixation |
| E | 0016984 | molecular_function | ribulose-bisphosphate carboxylase activity |
| E | 0019253 | biological_process | reductive pentose-phosphate cycle |
| F | 0009507 | cellular_component | chloroplast |
| F | 0015977 | biological_process | carbon fixation |
| F | 0016984 | molecular_function | ribulose-bisphosphate carboxylase activity |
| F | 0019253 | biological_process | reductive pentose-phosphate cycle |
| H | 0000287 | molecular_function | magnesium ion binding |
| H | 0009507 | cellular_component | chloroplast |
| H | 0015977 | biological_process | carbon fixation |
| H | 0016984 | molecular_function | ribulose-bisphosphate carboxylase activity |
| H | 0019253 | biological_process | reductive pentose-phosphate cycle |
| I | 0009507 | cellular_component | chloroplast |
| I | 0015977 | biological_process | carbon fixation |
| I | 0016984 | molecular_function | ribulose-bisphosphate carboxylase activity |
| I | 0019253 | biological_process | reductive pentose-phosphate cycle |
| K | 0000287 | molecular_function | magnesium ion binding |
| K | 0009507 | cellular_component | chloroplast |
| K | 0015977 | biological_process | carbon fixation |
| K | 0016984 | molecular_function | ribulose-bisphosphate carboxylase activity |
| K | 0019253 | biological_process | reductive pentose-phosphate cycle |
| L | 0000287 | molecular_function | magnesium ion binding |
| L | 0009507 | cellular_component | chloroplast |
| L | 0015977 | biological_process | carbon fixation |
| L | 0016984 | molecular_function | ribulose-bisphosphate carboxylase activity |
| L | 0019253 | biological_process | reductive pentose-phosphate cycle |
| M | 0009507 | cellular_component | chloroplast |
| M | 0015977 | biological_process | carbon fixation |
| M | 0016984 | molecular_function | ribulose-bisphosphate carboxylase activity |
| M | 0019253 | biological_process | reductive pentose-phosphate cycle |
| O | 0000287 | molecular_function | magnesium ion binding |
| O | 0009507 | cellular_component | chloroplast |
| O | 0015977 | biological_process | carbon fixation |
| O | 0016984 | molecular_function | ribulose-bisphosphate carboxylase activity |
| O | 0019253 | biological_process | reductive pentose-phosphate cycle |
| P | 0009507 | cellular_component | chloroplast |
| P | 0015977 | biological_process | carbon fixation |
| P | 0016984 | molecular_function | ribulose-bisphosphate carboxylase activity |
| P | 0019253 | biological_process | reductive pentose-phosphate cycle |
| R | 0000287 | molecular_function | magnesium ion binding |
| R | 0009507 | cellular_component | chloroplast |
| R | 0015977 | biological_process | carbon fixation |
| R | 0016984 | molecular_function | ribulose-bisphosphate carboxylase activity |
| R | 0019253 | biological_process | reductive pentose-phosphate cycle |
| S | 0009507 | cellular_component | chloroplast |
| S | 0015977 | biological_process | carbon fixation |
| S | 0016984 | molecular_function | ribulose-bisphosphate carboxylase activity |
| S | 0019253 | biological_process | reductive pentose-phosphate cycle |
| T | 0009507 | cellular_component | chloroplast |
| T | 0015977 | biological_process | carbon fixation |
| T | 0016984 | molecular_function | ribulose-bisphosphate carboxylase activity |
| T | 0019253 | biological_process | reductive pentose-phosphate cycle |
| V | 0000287 | molecular_function | magnesium ion binding |
| V | 0009507 | cellular_component | chloroplast |
| V | 0015977 | biological_process | carbon fixation |
| V | 0016984 | molecular_function | ribulose-bisphosphate carboxylase activity |
| V | 0019253 | biological_process | reductive pentose-phosphate cycle |
| W | 0009507 | cellular_component | chloroplast |
| W | 0015977 | biological_process | carbon fixation |
| W | 0016984 | molecular_function | ribulose-bisphosphate carboxylase activity |
| W | 0019253 | biological_process | reductive pentose-phosphate cycle |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE XDP L 476 |
| Chain | Residue |
| B | GLU60 |
| B | THR65 |
| B | TRP66 |
| B | ASN123 |
| B | HOH477 |
| L | LYS175 |
| L | LYS177 |
| L | ASP203 |
| L | GLU204 |
| L | ARG295 |
| L | HIS327 |
| L | LYS334 |
| L | LEU335 |
| L | SER379 |
| L | GLY380 |
| L | GLY381 |
| L | GLY403 |
| L | GLY404 |
| L | HOH496 |
| L | HOH504 |
| L | HOH507 |
| L | HOH521 |
| L | HOH564 |
| L | HOH579 |
| L | HOH585 |
| site_id | AC2 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE XDP B 476 |
| Chain | Residue |
| B | LYS175 |
| B | LYS177 |
| B | ASP203 |
| B | GLU204 |
| B | ARG295 |
| B | HIS327 |
| B | LYS334 |
| B | LEU335 |
| B | SER379 |
| B | GLY380 |
| B | GLY381 |
| B | GLY403 |
| B | GLY404 |
| B | HOH503 |
| B | HOH510 |
| B | HOH513 |
| B | HOH526 |
| B | HOH568 |
| B | HOH583 |
| B | HOH589 |
| L | GLU60 |
| L | THR65 |
| L | TRP66 |
| L | ASN123 |
| L | HOH654 |
| site_id | AC3 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE XDP E 476 |
| Chain | Residue |
| E | LYS175 |
| E | LYS177 |
| E | ASP203 |
| E | GLU204 |
| E | ARG295 |
| E | HIS327 |
| E | LYS334 |
| E | LEU335 |
| E | SER379 |
| E | GLY380 |
| E | GLY381 |
| E | GLY403 |
| E | GLY404 |
| E | HOH504 |
| E | HOH511 |
| E | HOH514 |
| E | HOH528 |
| E | HOH572 |
| E | HOH587 |
| E | HOH593 |
| H | GLU60 |
| H | THR65 |
| H | TRP66 |
| H | ASN123 |
| H | HOH483 |
| site_id | AC4 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE XDP H 476 |
| Chain | Residue |
| E | GLU60 |
| E | THR65 |
| E | TRP66 |
| E | ASN123 |
| E | HOH660 |
| H | LYS175 |
| H | LYS177 |
| H | ASP203 |
| H | GLU204 |
| H | ARG295 |
| H | HIS327 |
| H | LYS334 |
| H | LEU335 |
| H | SER379 |
| H | GLY380 |
| H | GLY381 |
| H | GLY403 |
| H | GLY404 |
| H | HOH510 |
| H | HOH518 |
| H | HOH521 |
| H | HOH535 |
| H | HOH579 |
| H | HOH594 |
| H | HOH600 |
| site_id | AC5 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE XDP K 476 |
| Chain | Residue |
| K | LYS175 |
| K | LYS177 |
| K | ASP203 |
| K | GLU204 |
| K | ARG295 |
| K | HIS327 |
| K | LYS334 |
| K | LEU335 |
| K | SER379 |
| K | GLY380 |
| K | GLY381 |
| K | GLY403 |
| K | GLY404 |
| K | HOH976 |
| K | HOH987 |
| K | HOH991 |
| K | HOH1010 |
| K | HOH1063 |
| K | HOH1087 |
| K | HOH1096 |
| O | GLU60 |
| O | THR65 |
| O | TRP66 |
| O | ASN123 |
| O | HOH953 |
| site_id | AC6 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE XDP O 476 |
| Chain | Residue |
| K | GLU60 |
| K | THR65 |
| K | TRP66 |
| K | ASN123 |
| K | HOH1191 |
| O | LYS175 |
| O | LYS177 |
| O | ASP203 |
| O | GLU204 |
| O | ARG295 |
| O | HIS327 |
| O | LYS334 |
| O | LEU335 |
| O | SER379 |
| O | GLY380 |
| O | GLY381 |
| O | GLY403 |
| O | GLY404 |
| O | HOH1214 |
| O | HOH1225 |
| O | HOH1229 |
| O | HOH1248 |
| O | HOH1301 |
| O | HOH1325 |
| O | HOH1334 |
| site_id | AC7 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE XDP R 476 |
| Chain | Residue |
| R | LYS175 |
| R | LYS177 |
| R | ASP203 |
| R | GLU204 |
| R | ARG295 |
| R | HIS327 |
| R | LYS334 |
| R | LEU335 |
| R | SER379 |
| R | GLY380 |
| R | GLY381 |
| R | GLY403 |
| R | GLY404 |
| R | HOH509 |
| R | HOH516 |
| R | HOH519 |
| R | HOH533 |
| R | HOH577 |
| R | HOH592 |
| R | HOH598 |
| V | GLU60 |
| V | THR65 |
| V | TRP66 |
| V | ASN123 |
| V | HOH490 |
| site_id | AC8 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE XDP V 476 |
| Chain | Residue |
| R | GLU60 |
| R | THR65 |
| R | TRP66 |
| V | LYS175 |
| V | LYS177 |
| V | ASP203 |
| V | GLU204 |
| V | ARG295 |
| V | HIS327 |
| V | LYS334 |
| V | LEU335 |
| V | SER379 |
| V | GLY380 |
| V | GLY381 |
| V | GLY403 |
| V | GLY404 |
| V | HOH498 |
| V | HOH518 |
| V | HOH526 |
| V | HOH529 |
| V | HOH544 |
| V | HOH586 |
| V | HOH602 |
| V | HOH608 |
| site_id | ACB |
| Number of Residues | 3 |
| Details | ACTIVE SITE. |
| Chain | Residue |
| B | LYS201 |
| B | ASP203 |
| L | GLU204 |
| site_id | ACE |
| Number of Residues | 3 |
| Details | ACTIVE SITE. |
| Chain | Residue |
| E | LYS201 |
| E | ASP203 |
| L | GLU204 |
| site_id | ACH |
| Number of Residues | 3 |
| Details | ACTIVE SITE. |
| Chain | Residue |
| H | LYS201 |
| H | ASP203 |
| L | GLU204 |
| site_id | ACK |
| Number of Residues | 3 |
| Details | ACTIVE SITE. |
| Chain | Residue |
| K | LYS201 |
| K | ASP203 |
| L | GLU204 |
| site_id | ACL |
| Number of Residues | 3 |
| Details | ACTIVE SITE. |
| Chain | Residue |
| L | LYS201 |
| L | ASP203 |
| L | GLU204 |
| site_id | ACO |
| Number of Residues | 3 |
| Details | ACTIVE SITE. |
| Chain | Residue |
| O | LYS201 |
| O | ASP203 |
| L | GLU204 |
| site_id | ACR |
| Number of Residues | 3 |
| Details | ACTIVE SITE. |
| Chain | Residue |
| R | LYS201 |
| R | ASP203 |
| L | GLU204 |
| site_id | ACV |
| Number of Residues | 3 |
| Details | ACTIVE SITE. |
| Chain | Residue |
| V | LYS201 |
| V | ASP203 |
| L | GLU204 |
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 |
| L | GLY196-GLU204 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 8 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"2118958","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"637859","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9092835","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"637859","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 40 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"9034362","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1RCX","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 8 |
| Details | Binding site: {"description":"in homodimeric partner","evidences":[{"source":"PubMed","id":"9034362","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1RCX","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 24 |
| Details | Binding site: {} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 8 |
| Details | Binding site: {"description":"via carbamate group","evidences":[{"source":"PubMed","id":"8648644","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9092835","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"14596800","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"2118958","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"9034362","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"8648644","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9092835","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"14596800","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"2118958","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"9034362","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"9034362","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1RXO","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 24 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"9034362","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1RCX","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1RXO","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 8 |
| Details | Site: {"description":"Not N6-methylated","evidences":[{"source":"PubMed","id":"2928307","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI11 |
| Number of Residues | 8 |
| Details | Site: {"description":"Transition state stabilizer","evidences":[{"source":"PubMed","id":"8955130","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI12 |
| Number of Residues | 8 |
| Details | Modified residue: {"description":"N6-carboxylysine","evidences":[{"source":"PubMed","id":"14596800","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"2118958","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8648644","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9034362","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9092835","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI13 |
| Number of Residues | 8 |
| Details | Modified residue: {"description":"Methionine derivative"} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 6 |
| Details | Annotated By Reference To The Literature 1rbl |
| Chain | Residue | Details |
| L | LYS175 | |
| L | LYS201 | |
| L | LYS177 | |
| L | HIS294 | |
| L | ASP203 | |
| L | HIS327 |
| site_id | CSA2 |
| Number of Residues | 6 |
| Details | Annotated By Reference To The Literature 1rbl |
| Chain | Residue | Details |
| B | LYS175 | |
| B | LYS201 | |
| B | LYS177 | |
| B | HIS294 | |
| B | ASP203 | |
| B | HIS327 |
| site_id | CSA3 |
| Number of Residues | 6 |
| Details | Annotated By Reference To The Literature 1rbl |
| Chain | Residue | Details |
| E | LYS175 | |
| E | LYS201 | |
| E | LYS177 | |
| E | HIS294 | |
| E | ASP203 | |
| E | HIS327 |
| site_id | CSA4 |
| Number of Residues | 6 |
| Details | Annotated By Reference To The Literature 1rbl |
| Chain | Residue | Details |
| H | LYS175 | |
| H | LYS201 | |
| H | LYS177 | |
| H | HIS294 | |
| H | ASP203 | |
| H | HIS327 |
| site_id | CSA5 |
| Number of Residues | 6 |
| Details | Annotated By Reference To The Literature 1rbl |
| Chain | Residue | Details |
| K | LYS175 | |
| K | LYS201 | |
| K | LYS177 | |
| K | HIS294 | |
| K | ASP203 | |
| K | HIS327 |
| site_id | CSA6 |
| Number of Residues | 6 |
| Details | Annotated By Reference To The Literature 1rbl |
| Chain | Residue | Details |
| O | LYS175 | |
| O | LYS201 | |
| O | LYS177 | |
| O | HIS294 | |
| O | ASP203 | |
| O | HIS327 |
| site_id | CSA7 |
| Number of Residues | 6 |
| Details | Annotated By Reference To The Literature 1rbl |
| Chain | Residue | Details |
| R | LYS175 | |
| R | LYS201 | |
| R | LYS177 | |
| R | HIS294 | |
| R | ASP203 | |
| R | HIS327 |
| site_id | CSA8 |
| Number of Residues | 6 |
| Details | Annotated By Reference To The Literature 1rbl |
| Chain | Residue | Details |
| V | LYS175 | |
| V | LYS201 | |
| V | LYS177 | |
| V | HIS294 | |
| V | ASP203 | |
| V | HIS327 |






