Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000287 | molecular_function | magnesium ion binding |
A | 0004497 | molecular_function | monooxygenase activity |
A | 0009507 | cellular_component | chloroplast |
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 | 0046872 | molecular_function | metal ion binding |
B | 0000287 | molecular_function | magnesium ion binding |
B | 0004497 | molecular_function | monooxygenase activity |
B | 0009507 | cellular_component | chloroplast |
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 | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
site_id | CAT |
Number of Residues | 10 |
Details | CATALYTIC SITE |
Chain | Residue |
A | LYS175 |
A | SER379 |
A | LYS201 |
A | LYS177 |
A | ASP203 |
A | GLU204 |
A | HIS294 |
A | HIS327 |
A | ARG295 |
A | HIS298 |
Functional Information from PROSITE/UniProt
site_id | PS00018 |
Number of Residues | 13 |
Details | EF_HAND_1 EF-hand calcium-binding domain. DLSQEQLLSevEY |
Chain | Residue | Details |
S | ASP520-TYR532 | |
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 | ACT_SITE: Proton acceptor |
Chain | Residue | Details |
A | LYS175 | |
A | HIS294 | |
B | LYS175 | |
B | HIS294 | |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | BINDING: in homodimeric partner |
Chain | Residue | Details |
A | ASN123 | |
B | ASN123 | |
site_id | SWS_FT_FI3 |
Number of Residues | 14 |
Details | BINDING: |
Chain | Residue | Details |
A | THR173 | |
B | ASP203 | |
B | GLU204 | |
B | ARG295 | |
B | HIS327 | |
B | SER379 | |
A | LYS177 | |
A | ASP203 | |
A | GLU204 | |
A | ARG295 | |
A | HIS327 | |
A | SER379 | |
B | THR173 | |
B | LYS177 | |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | BINDING: via carbamate group |
Chain | Residue | Details |
A | LYS201 | |
B | LYS201 | |
site_id | SWS_FT_FI5 |
Number of Residues | 2 |
Details | SITE: Transition state stabilizer |
Chain | Residue | Details |
A | LYS334 | |
B | LYS334 | |
Chain | Residue | Details |
A | LYS201 | |
B | LYS201 | |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 6 |
Details | Annotated By Reference To The Literature 1rbl |
Chain | Residue | Details |
A | LYS175 | |
A | LYS201 | |
A | LYS177 | |
A | HIS294 | |
A | ASP203 | |
A | 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 | |