3GDN
Almond hydroxynitrile lyase in complex with benzaldehyde
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0016614 | molecular_function | oxidoreductase activity, acting on CH-OH group of donors |
A | 0016829 | molecular_function | lyase activity |
A | 0046593 | molecular_function | mandelonitrile lyase activity |
A | 0050660 | molecular_function | flavin adenine dinucleotide binding |
A | 0050898 | biological_process | nitrile metabolic process |
B | 0016614 | molecular_function | oxidoreductase activity, acting on CH-OH group of donors |
B | 0016829 | molecular_function | lyase activity |
B | 0046593 | molecular_function | mandelonitrile lyase activity |
B | 0050660 | molecular_function | flavin adenine dinucleotide binding |
B | 0050898 | biological_process | nitrile metabolic process |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | Active site: {"description":"Proton donor"} |
Chain | Residue | Details |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | Active site: {"description":"Proton acceptor"} |
Chain | Residue | Details |
site_id | SWS_FT_FI3 |
Number of Residues | 22 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"19256550","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI4 |
Number of Residues | 4 |
Details | Binding site: {} |
Chain | Residue | Details |
site_id | SWS_FT_FI5 |
Number of Residues | 8 |
Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"11566130","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19256550","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
Catalytic Information from CSA
site_id | MCSA1 |
Number of Residues | 6 |
Details | M-CSA 941 |
Chain | Residue | Details |
A | CYS328 | electrostatic stabiliser, modifies pKa |
A | LYS361 | electrostatic stabiliser, modifies pKa |
A | TYR457 | electrostatic stabiliser, modifies pKa |
A | HIS459 | electrostatic stabiliser |
A | SER496 | electrostatic stabiliser, modifies pKa |
A | HIS497 | proton acceptor, proton donor |
site_id | MCSA2 |
Number of Residues | 6 |
Details | M-CSA 941 |
Chain | Residue | Details |
B | CYS328 | electrostatic stabiliser, modifies pKa |
B | LYS361 | electrostatic stabiliser, modifies pKa |
B | TYR457 | electrostatic stabiliser, modifies pKa |
B | HIS459 | electrostatic stabiliser |
B | SER496 | electrostatic stabiliser, modifies pKa |
B | HIS497 | proton acceptor, proton donor |