5RUB
CRYSTALLOGRAPHIC REFINEMENT AND STRUCTURE OF RIBULOSE-1,5-BISPHOSPHATE CARBOXYLASE FROM RHODOSPIRILLUM RUBRUM AT 1.7 ANGSTROMS RESOLUTION
Replaces: 2RUBFunctional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0004497 | molecular_function | monooxygenase activity |
| 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 | 0000287 | molecular_function | magnesium ion binding |
| B | 0004497 | molecular_function | monooxygenase activity |
| 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 PROSITE/UniProt
| site_id | PS00157 |
| Number of Residues | 9 |
| Details | RUBISCO_LARGE Ribulose bisphosphate carboxylase large chain active site. GgDFiKnDE |
| Chain | Residue | Details |
| A | GLY186-GLU194 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | Active site: {"description":"Proton acceptor"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Binding site: {"description":"in homodimeric partner"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 8 |
| Details | Binding site: {} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Binding site: {"description":"via carbamate group","evidences":[{"source":"PubMed","id":"1899197","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"journal article","publicationDate":"1989","firstPage":"229","lastPage":"234","volume":"337","journal":"Nature","title":"Crystal structure of the active site of ribulose-bisphosphate carboxylase.","authors":["Andersson I.","Knight S.","Schneider G.","Lindqvist Y.","Lundqvist T.","Braenden C.-I.","Lorimer G.H."]}}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"1899197","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"journal article","publicationDate":"1989","firstPage":"229","lastPage":"234","volume":"337","journal":"Nature","title":"Crystal structure of the active site of ribulose-bisphosphate carboxylase.","authors":["Andersson I.","Knight S.","Schneider G.","Lindqvist Y.","Lundqvist T.","Braenden C.-I.","Lorimer G.H."]}}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-carboxylysine","evidences":[{"source":"PubMed","id":"1899197","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 5 |
| Details | Annotated By Reference To The Literature 1rbl |
| Chain | Residue | Details |
| A | ASN192 | |
| A | HIS287 | |
| A | LYS166 | |
| A | LYS191 | |
| A | HIS321 |
| site_id | CSA2 |
| Number of Residues | 5 |
| Details | Annotated By Reference To The Literature 1rbl |
| Chain | Residue | Details |
| B | ASN192 | |
| B | HIS287 | |
| B | LYS166 | |
| B | LYS191 | |
| B | HIS321 |
| site_id | CSA3 |
| Number of Residues | 6 |
| Details | Annotated By Reference To The Literature 1rbl |
| Chain | Residue | Details |
| A | HIS287 | |
| A | LYS166 | |
| A | ASP193 | |
| A | LYS191 | |
| A | HIS321 | |
| A | LYS168 |
| site_id | CSA4 |
| Number of Residues | 6 |
| Details | Annotated By Reference To The Literature 1rbl |
| Chain | Residue | Details |
| B | HIS287 | |
| B | LYS166 | |
| B | ASP193 | |
| B | LYS191 | |
| B | HIS321 | |
| B | LYS168 |
| site_id | MCSA1 |
| Number of Residues | 7 |
| Details | M-CSA 797 |
| Chain | Residue | Details |
| A | LYS166 | electrostatic stabiliser, proton acceptor, proton donor |
| A | LYS191 | electron pair donor, metal ligand, nucleophile |
| A | ASN192 | electrostatic stabiliser |
| A | ASP193 | metal ligand |
| A | GLU194 | metal ligand |
| A | HIS287 | activator, increase nucleophilicity, proton acceptor |
| A | HIS321 | electrostatic stabiliser |
| site_id | MCSA2 |
| Number of Residues | 7 |
| Details | M-CSA 797 |
| Chain | Residue | Details |
| B | LYS166 | electrostatic stabiliser, proton acceptor, proton donor |
| B | LYS191 | electron pair donor, metal ligand, nucleophile |
| B | ASN192 | electrostatic stabiliser |
| B | ASP193 | metal ligand |
| B | GLU194 | metal ligand |
| B | HIS287 | activator, increase nucleophilicity, proton acceptor |
| B | HIS321 | electrostatic stabiliser |
