1JU2
Crystal structure of the hydroxynitrile lyase from almond
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 | ACT_SITE: Proton donor |
| Chain | Residue | Details |
| A | HIS459 | |
| B | HIS459 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton acceptor |
| Chain | Residue | Details |
| A | HIS497 | |
| B | HIS497 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 18 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:19256550 |
| Chain | Residue | Details |
| A | THR36 | |
| B | THR36 | |
| B | GLU55 | |
| B | VAL102 | |
| B | THR106 | |
| B | ASN110 | |
| B | VAL217 | |
| B | TRP458 | |
| B | GLY487 | |
| B | PRO498 | |
| A | GLU55 | |
| A | VAL102 | |
| A | THR106 | |
| A | ASN110 | |
| A | VAL217 | |
| A | TRP458 | |
| A | GLY487 | |
| A | PRO498 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | CYS328 | |
| A | TYR457 | |
| B | CYS328 | |
| B | TYR457 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 8 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:11566130, ECO:0000269|PubMed:19256550 |
| Chain | Residue | Details |
| A | ASN118 | |
| A | ASN135 | |
| A | ASN352 | |
| A | ASN392 | |
| B | ASN118 | |
| B | ASN135 | |
| B | ASN352 | |
| B | ASN392 |
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 |
