1RBA
SUBSTITUTION OF ASP193 TO ASN AT THE ACTIVE SITE OF RIBULOSE-1,5-BISPHOSPHATE CARBOXYLASE RESULTS IN CONFORMATIONAL CHANGES
Functional 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 | 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 | 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 SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 4 |
Details | ACT_SITE: Proton acceptor |
Chain | Residue | Details |
A | LYS166 | |
A | HIS287 | |
B | LYS166 | |
B | HIS287 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | BINDING: in homodimeric partner |
Chain | Residue | Details |
A | ASN111 | |
B | ASN111 |
site_id | SWS_FT_FI3 |
Number of Residues | 8 |
Details | BINDING: |
Chain | Residue | Details |
A | LYS168 | |
A | ARG288 | |
A | HIS321 | |
A | SER368 | |
B | LYS168 | |
B | ARG288 | |
B | HIS321 | |
B | SER368 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | BINDING: via carbamate group => ECO:0000269|PubMed:1899197, ECO:0000269|Ref.4 |
Chain | Residue | Details |
A | LYS191 | |
B | LYS191 |
site_id | SWS_FT_FI5 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000269|PubMed:1899197, ECO:0000269|Ref.4 |
Chain | Residue | Details |
A | ASN193 | |
A | GLU194 | |
B | ASN193 | |
B | GLU194 |
site_id | SWS_FT_FI6 |
Number of Residues | 2 |
Details | SITE: Transition state stabilizer |
Chain | Residue | Details |
A | LYS329 | |
B | LYS329 |
site_id | SWS_FT_FI7 |
Number of Residues | 2 |
Details | MOD_RES: N6-carboxylysine => ECO:0000269|PubMed:1899197 |
Chain | Residue | Details |
A | LYS191 | |
B | LYS191 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 5 |
Details | a catalytic site defined by CSA, PubMed 3129424, 2991249, 6778504, 8909282, 8648644, 2545684, 3151016, 1761567, 6784749, 11848907 |
Chain | Residue | Details |
A | ASN192 | |
A | HIS287 | |
A | LYS166 | |
A | LYS191 | |
A | HIS321 |
site_id | CSA2 |
Number of Residues | 5 |
Details | a catalytic site defined by CSA, PubMed 3129424, 2991249, 6778504, 8909282, 8648644, 2545684, 3151016, 1761567, 6784749, 11848907 |
Chain | Residue | Details |
B | ASN192 | |
B | HIS287 | |
B | LYS166 | |
B | LYS191 | |
B | HIS321 |
site_id | MCSA1 |
Number of Residues | 8 |
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 | ASN193 | metal ligand |
A | GLU194 | metal ligand |
A | HIS287 | activator, increase nucleophilicity, proton acceptor |
A | HIS321 | electrostatic stabiliser |
A | LYS329 | electrostatic stabiliser |
site_id | MCSA2 |
Number of Residues | 8 |
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 | ASN193 | metal ligand |
B | GLU194 | metal ligand |
B | HIS287 | activator, increase nucleophilicity, proton acceptor |
B | HIS321 | electrostatic stabiliser |
B | LYS329 | electrostatic stabiliser |