1BXN
THE CRYSTAL STRUCTURE OF RUBISCO FROM ALCALIGENES EUTROPHUS TO 2.7 ANGSTROMS.
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0015977 | biological_process | carbon fixation |
| A | 0016984 | molecular_function | ribulose-bisphosphate carboxylase activity |
| A | 0019253 | biological_process | reductive pentose-phosphate cycle |
| C | 0000287 | molecular_function | magnesium ion binding |
| 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 | 0015977 | biological_process | carbon fixation |
| E | 0016984 | molecular_function | ribulose-bisphosphate carboxylase activity |
| E | 0019253 | biological_process | reductive pentose-phosphate cycle |
| G | 0000287 | molecular_function | magnesium ion binding |
| G | 0015977 | biological_process | carbon fixation |
| G | 0016984 | molecular_function | ribulose-bisphosphate carboxylase activity |
| G | 0019253 | biological_process | reductive pentose-phosphate cycle |
| I | 0015977 | biological_process | carbon fixation |
| I | 0016984 | molecular_function | ribulose-bisphosphate carboxylase activity |
| I | 0019253 | biological_process | reductive pentose-phosphate cycle |
| J | 0015977 | biological_process | carbon fixation |
| J | 0016984 | molecular_function | ribulose-bisphosphate carboxylase activity |
| J | 0019253 | biological_process | reductive pentose-phosphate cycle |
| K | 0015977 | biological_process | carbon fixation |
| K | 0016984 | molecular_function | ribulose-bisphosphate carboxylase activity |
| K | 0019253 | biological_process | reductive pentose-phosphate cycle |
| L | 0015977 | biological_process | carbon fixation |
| L | 0016984 | molecular_function | ribulose-bisphosphate carboxylase activity |
| L | 0019253 | biological_process | reductive pentose-phosphate cycle |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PO4 A 501 |
| Chain | Residue |
| A | ARG297 |
| A | HIS329 |
| A | GLU338 |
| A | SER381 |
| E | ASN126 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PO4 A 502 |
| Chain | Residue |
| E | TRP69 |
| A | GLY382 |
| A | GLY405 |
| A | GLY406 |
| E | THR68 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE PO4 C 503 |
| Chain | Residue |
| C | ARG297 |
| C | HIS329 |
| C | GLU338 |
| C | SER381 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE PO4 C 504 |
| Chain | Residue |
| C | THR68 |
| C | TRP69 |
| C | GLY382 |
| C | GLY383 |
| C | GLY405 |
| C | GLY406 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE PO4 E 505 |
| Chain | Residue |
| E | ARG297 |
| E | HIS329 |
| E | GLU338 |
| E | SER381 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PO4 E 506 |
| Chain | Residue |
| A | THR68 |
| A | TRP69 |
| E | GLY382 |
| E | GLY405 |
| E | GLY406 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE PO4 G 507 |
| Chain | Residue |
| G | ARG297 |
| G | HIS329 |
| G | GLU338 |
| G | SER381 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE PO4 G 508 |
| Chain | Residue |
| G | THR68 |
| G | TRP69 |
| G | GLY405 |
| G | GLY406 |
Functional Information from PROSITE/UniProt
| site_id | PS00157 |
| Number of Residues | 9 |
| Details | RUBISCO_LARGE Ribulose bisphosphate carboxylase large chain active site. GlDFmKdDE |
| Chain | Residue | Details |
| A | GLY199-GLU207 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 8 |
| Details | Active site: {"description":"Proton acceptor"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | Binding site: {"description":"in homodimeric partner"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 28 |
| Details | Binding site: {} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | Binding site: {"description":"via carbamate group"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | Site: {"description":"Transition state stabilizer"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"N6-carboxylysine","evidences":[{"source":"PubMed","id":"2820933","evidenceCode":"ECO:0000269"}]} |
| 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 |
| A | LYS204 | |
| A | ASP206 | |
| A | LYS180 | |
| A | HIS329 | |
| A | HIS296 | |
| A | LYS178 |
| site_id | CSA2 |
| Number of Residues | 6 |
| Details | Annotated By Reference To The Literature 1rbl |
| Chain | Residue | Details |
| C | LYS204 | |
| C | ASP206 | |
| C | LYS180 | |
| C | HIS329 | |
| C | HIS296 | |
| C | LYS178 |
| site_id | CSA3 |
| Number of Residues | 6 |
| Details | Annotated By Reference To The Literature 1rbl |
| Chain | Residue | Details |
| E | LYS204 | |
| E | ASP206 | |
| E | LYS180 | |
| E | HIS329 | |
| E | HIS296 | |
| E | LYS178 |
| site_id | CSA4 |
| Number of Residues | 6 |
| Details | Annotated By Reference To The Literature 1rbl |
| Chain | Residue | Details |
| G | LYS204 | |
| G | ASP206 | |
| G | LYS180 | |
| G | HIS329 | |
| G | HIS296 | |
| G | LYS178 |
