Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003824 | molecular_function | catalytic activity |
A | 0004333 | molecular_function | fumarate hydratase activity |
A | 0005737 | cellular_component | cytoplasm |
A | 0006099 | biological_process | tricarboxylic acid cycle |
A | 0006106 | biological_process | fumarate metabolic process |
A | 0006108 | biological_process | malate metabolic process |
A | 0006979 | biological_process | response to oxidative stress |
A | 0016829 | molecular_function | lyase activity |
A | 0042802 | molecular_function | identical protein binding |
B | 0003824 | molecular_function | catalytic activity |
B | 0004333 | molecular_function | fumarate hydratase activity |
B | 0005737 | cellular_component | cytoplasm |
B | 0006099 | biological_process | tricarboxylic acid cycle |
B | 0006106 | biological_process | fumarate metabolic process |
B | 0006108 | biological_process | malate metabolic process |
B | 0006979 | biological_process | response to oxidative stress |
B | 0016829 | molecular_function | lyase activity |
B | 0042802 | molecular_function | identical protein binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 11 |
Details | binding site for residue CIT A 501 |
Chain | Residue |
A | THR100 |
B | THR187 |
B | HIS188 |
A | SER139 |
A | SER140 |
A | ASN141 |
A | LYS324 |
A | ASN326 |
A | HOH604 |
A | HOH609 |
A | HOH627 |
site_id | AC2 |
Number of Residues | 5 |
Details | binding site for residue CIT A 502 |
Chain | Residue |
A | ARG126 |
A | HIS129 |
A | PRO130 |
A | ASN131 |
A | ASP132 |
site_id | AC3 |
Number of Residues | 8 |
Details | binding site for residue CIT B 501 |
Chain | Residue |
B | MET124 |
B | ARG126 |
B | HIS129 |
B | PRO130 |
B | ASN131 |
B | ASP132 |
B | HOH624 |
B | HOH772 |
site_id | AC4 |
Number of Residues | 9 |
Details | binding site for residue CIT B 502 |
Chain | Residue |
A | THR187 |
B | THR100 |
B | SER139 |
B | SER140 |
B | ASN141 |
B | LYS324 |
B | ASN326 |
B | HOH601 |
B | HOH604 |
Functional Information from PROSITE/UniProt
site_id | PS00163 |
Number of Residues | 10 |
Details | FUMARATE_LYASES Fumarate lyases signature. GSsiMpGKvN |
Chain | Residue | Details |
A | GLY317-ASN326 | |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
A | HIS188 | |
B | HIS188 | |
Chain | Residue | Details |
A | SER318 | |
B | SER318 | |
Chain | Residue | Details |
A | SER98 | |
B | SER98 | |
Chain | Residue | Details |
A | ARG126 | |
B | ARG126 | |
Chain | Residue | Details |
A | HIS129 | |
B | HIS129 | |
Chain | Residue | Details |
A | SER139 | |
B | SER139 | |
Chain | Residue | Details |
A | THR187 | |
A | SER319 | |
A | LYS324 | |
B | THR187 | |
B | SER319 | |
B | LYS324 | |
Chain | Residue | Details |
A | GLU331 | |
B | GLU331 | |
Catalytic Information from CSA
site_id | MCSA1 |
Number of Residues | 4 |
Details | M-CSA 569 |
Chain | Residue | Details |
A | HIS188 | electrostatic stabiliser, proton acceptor |
A | SER318 | proton donor |
A | LYS324 | electrostatic stabiliser |
A | GLU331 | increase basicity |
site_id | MCSA2 |
Number of Residues | 4 |
Details | M-CSA 569 |
Chain | Residue | Details |
B | HIS188 | electrostatic stabiliser, proton acceptor |
B | SER318 | proton donor |
B | LYS324 | electrostatic stabiliser |
B | GLU331 | increase basicity |