3RED
3.0 A structure of the Prunus mume hydroxynitrile lyase isozyme-1
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0016491 | molecular_function | oxidoreductase activity |
| 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 |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0016491 | molecular_function | oxidoreductase activity |
| 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 |
| C | 0000166 | molecular_function | nucleotide binding |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0016614 | molecular_function | oxidoreductase activity, acting on CH-OH group of donors |
| C | 0016829 | molecular_function | lyase activity |
| C | 0046593 | molecular_function | mandelonitrile lyase activity |
| C | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| D | 0000166 | molecular_function | nucleotide binding |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0016614 | molecular_function | oxidoreductase activity, acting on CH-OH group of donors |
| D | 0016829 | molecular_function | lyase activity |
| D | 0046593 | molecular_function | mandelonitrile lyase activity |
| D | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| E | 0000166 | molecular_function | nucleotide binding |
| E | 0016491 | molecular_function | oxidoreductase activity |
| E | 0016614 | molecular_function | oxidoreductase activity, acting on CH-OH group of donors |
| E | 0016829 | molecular_function | lyase activity |
| E | 0046593 | molecular_function | mandelonitrile lyase activity |
| E | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| F | 0000166 | molecular_function | nucleotide binding |
| F | 0016491 | molecular_function | oxidoreductase activity |
| F | 0016614 | molecular_function | oxidoreductase activity, acting on CH-OH group of donors |
| F | 0016829 | molecular_function | lyase activity |
| F | 0046593 | molecular_function | mandelonitrile lyase activity |
| F | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| G | 0000166 | molecular_function | nucleotide binding |
| G | 0016491 | molecular_function | oxidoreductase activity |
| G | 0016614 | molecular_function | oxidoreductase activity, acting on CH-OH group of donors |
| G | 0016829 | molecular_function | lyase activity |
| G | 0046593 | molecular_function | mandelonitrile lyase activity |
| G | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| H | 0000166 | molecular_function | nucleotide binding |
| H | 0016491 | molecular_function | oxidoreductase activity |
| H | 0016614 | molecular_function | oxidoreductase activity, acting on CH-OH group of donors |
| H | 0016829 | molecular_function | lyase activity |
| H | 0046593 | molecular_function | mandelonitrile lyase activity |
| H | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| I | 0000166 | molecular_function | nucleotide binding |
| I | 0016491 | molecular_function | oxidoreductase activity |
| I | 0016614 | molecular_function | oxidoreductase activity, acting on CH-OH group of donors |
| I | 0016829 | molecular_function | lyase activity |
| I | 0046593 | molecular_function | mandelonitrile lyase activity |
| I | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| J | 0000166 | molecular_function | nucleotide binding |
| J | 0016491 | molecular_function | oxidoreductase activity |
| J | 0016614 | molecular_function | oxidoreductase activity, acting on CH-OH group of donors |
| J | 0016829 | molecular_function | lyase activity |
| J | 0046593 | molecular_function | mandelonitrile lyase activity |
| J | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| K | 0000166 | molecular_function | nucleotide binding |
| K | 0016491 | molecular_function | oxidoreductase activity |
| K | 0016614 | molecular_function | oxidoreductase activity, acting on CH-OH group of donors |
| K | 0016829 | molecular_function | lyase activity |
| K | 0046593 | molecular_function | mandelonitrile lyase activity |
| K | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| L | 0000166 | molecular_function | nucleotide binding |
| L | 0016491 | molecular_function | oxidoreductase activity |
| L | 0016614 | molecular_function | oxidoreductase activity, acting on CH-OH group of donors |
| L | 0016829 | molecular_function | lyase activity |
| L | 0046593 | molecular_function | mandelonitrile lyase activity |
| L | 0050660 | molecular_function | flavin adenine dinucleotide binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 26 |
| Details | BINDING SITE FOR RESIDUE FAD A 773 |
| Chain | Residue |
| A | GLY33 |
| A | GLY105 |
| A | THR106 |
| A | ASN110 |
| A | ALA111 |
| A | GLY112 |
| A | VAL113 |
| A | ALA215 |
| A | VAL217 |
| A | ALA258 |
| A | GLY259 |
| A | GLY35 |
| A | TRP459 |
| A | ASP487 |
| A | GLY488 |
| A | HIS498 |
| A | PRO499 |
| A | GLN500 |
| A | TYR503 |
| A | THR36 |
| A | SER37 |
| A | GLU55 |
| A | ARG56 |
| A | VAL98 |
| A | ARG101 |
| A | VAL102 |
| site_id | AC2 |
| Number of Residues | 29 |
| Details | BINDING SITE FOR RESIDUE FAD B 773 |
| Chain | Residue |
| B | GLY33 |
| B | GLY35 |
| B | THR36 |
| B | SER37 |
| B | GLU55 |
| B | ARG56 |
| B | VAL98 |
| B | GLY100 |
| B | ARG101 |
| B | VAL102 |
| B | GLY105 |
| B | THR106 |
| B | ASN110 |
| B | ALA111 |
| B | GLY112 |
| B | VAL113 |
| B | ALA215 |
| B | VAL217 |
| B | SER257 |
| B | ALA258 |
| B | VAL380 |
| B | TRP459 |
| B | HIS460 |
| B | ASP487 |
| B | GLY488 |
| B | HIS498 |
| B | PRO499 |
| B | GLN500 |
| B | TYR503 |
| site_id | AC3 |
| Number of Residues | 27 |
| Details | BINDING SITE FOR RESIDUE FAD C 773 |
| Chain | Residue |
| C | GLY33 |
| C | GLY35 |
| C | THR36 |
| C | SER37 |
| C | GLU55 |
| C | ARG56 |
| C | VAL98 |
| C | GLY100 |
| C | ARG101 |
| C | VAL102 |
| C | GLY105 |
| C | THR106 |
| C | ASN110 |
| C | ALA111 |
| C | GLY112 |
| C | VAL113 |
| C | ALA215 |
| C | VAL217 |
| C | SER257 |
| C | ALA258 |
| C | TRP459 |
| C | HIS460 |
| C | ASP487 |
| C | GLY488 |
| C | HIS498 |
| C | PRO499 |
| C | GLN500 |
| site_id | AC4 |
| Number of Residues | 29 |
| Details | BINDING SITE FOR RESIDUE FAD D 773 |
| Chain | Residue |
| D | VAL217 |
| D | SER257 |
| D | ALA258 |
| D | GLY259 |
| D | VAL380 |
| D | TRP459 |
| D | ASP487 |
| D | GLY488 |
| D | HIS498 |
| D | PRO499 |
| D | GLN500 |
| D | TYR503 |
| D | GLY33 |
| D | GLY35 |
| D | THR36 |
| D | SER37 |
| D | LEU54 |
| D | GLU55 |
| D | ARG56 |
| D | VAL98 |
| D | GLY100 |
| D | ARG101 |
| D | VAL102 |
| D | GLY105 |
| D | THR106 |
| D | ASN110 |
| D | ALA111 |
| D | GLY112 |
| D | VAL113 |
| site_id | AC5 |
| Number of Residues | 27 |
| Details | BINDING SITE FOR RESIDUE FAD E 773 |
| Chain | Residue |
| E | GLY33 |
| E | GLY35 |
| E | THR36 |
| E | SER37 |
| E | GLU55 |
| E | ARG56 |
| E | VAL98 |
| E | GLY100 |
| E | ARG101 |
| E | GLY105 |
| E | THR106 |
| E | ASN110 |
| E | ALA111 |
| E | GLY112 |
| E | VAL113 |
| E | ALA215 |
| E | VAL217 |
| E | SER257 |
| E | ALA258 |
| E | VAL380 |
| E | TRP459 |
| E | HIS460 |
| E | ASP487 |
| E | GLY488 |
| E | HIS498 |
| E | PRO499 |
| E | GLN500 |
| site_id | AC6 |
| Number of Residues | 27 |
| Details | BINDING SITE FOR RESIDUE FAD F 773 |
| Chain | Residue |
| F | GLY33 |
| F | GLY35 |
| F | THR36 |
| F | SER37 |
| F | LEU54 |
| F | GLU55 |
| F | ARG56 |
| F | VAL98 |
| F | GLY100 |
| F | ARG101 |
| F | VAL102 |
| F | GLY105 |
| F | THR106 |
| F | ASN110 |
| F | ALA111 |
| F | GLY112 |
| F | VAL113 |
| F | ALA215 |
| F | VAL217 |
| F | VAL380 |
| F | TRP459 |
| F | HIS460 |
| F | ASP487 |
| F | GLY488 |
| F | HIS498 |
| F | PRO499 |
| F | GLN500 |
| site_id | AC7 |
| Number of Residues | 29 |
| Details | BINDING SITE FOR RESIDUE FAD G 773 |
| Chain | Residue |
| G | GLY33 |
| G | GLY35 |
| G | THR36 |
| G | SER37 |
| G | GLU55 |
| G | ARG56 |
| G | VAL98 |
| G | GLY100 |
| G | ARG101 |
| G | VAL102 |
| G | GLY105 |
| G | THR106 |
| G | SER107 |
| G | ASN110 |
| G | ALA111 |
| G | GLY112 |
| G | VAL113 |
| G | VAL217 |
| G | SER257 |
| G | ALA258 |
| G | VAL380 |
| G | TRP459 |
| G | HIS460 |
| G | ASP487 |
| G | GLY488 |
| G | HIS498 |
| G | PRO499 |
| G | GLN500 |
| G | TYR503 |
| site_id | AC8 |
| Number of Residues | 31 |
| Details | BINDING SITE FOR RESIDUE FAD H 773 |
| Chain | Residue |
| H | GLY33 |
| H | GLY35 |
| H | THR36 |
| H | SER37 |
| H | GLU55 |
| H | ARG56 |
| H | VAL98 |
| H | GLY100 |
| H | ARG101 |
| H | VAL102 |
| H | GLY105 |
| H | THR106 |
| H | ASN110 |
| H | ALA111 |
| H | GLY112 |
| H | VAL113 |
| H | ALA215 |
| H | VAL217 |
| H | SER257 |
| H | ALA258 |
| H | GLY259 |
| H | PRO260 |
| H | VAL380 |
| H | TRP459 |
| H | HIS460 |
| H | ASP487 |
| H | GLY488 |
| H | HIS498 |
| H | PRO499 |
| H | GLN500 |
| H | TYR503 |
| site_id | AC9 |
| Number of Residues | 29 |
| Details | BINDING SITE FOR RESIDUE FAD I 773 |
| Chain | Residue |
| I | GLY33 |
| I | GLY35 |
| I | THR36 |
| I | SER37 |
| I | GLU55 |
| I | ARG56 |
| I | VAL98 |
| I | GLY100 |
| I | ARG101 |
| I | VAL102 |
| I | GLY105 |
| I | THR106 |
| I | ASN110 |
| I | ALA111 |
| I | GLY112 |
| I | VAL113 |
| I | ALA215 |
| I | VAL217 |
| I | SER257 |
| I | ALA258 |
| I | VAL380 |
| I | TRP459 |
| I | HIS460 |
| I | ASP487 |
| I | GLY488 |
| I | HIS498 |
| I | PRO499 |
| I | GLN500 |
| I | TYR503 |
| site_id | BC1 |
| Number of Residues | 28 |
| Details | BINDING SITE FOR RESIDUE FAD J 773 |
| Chain | Residue |
| J | GLY33 |
| J | GLY35 |
| J | THR36 |
| J | SER37 |
| J | GLU55 |
| J | ARG56 |
| J | VAL98 |
| J | GLY100 |
| J | VAL102 |
| J | GLY105 |
| J | THR106 |
| J | ASN110 |
| J | ALA111 |
| J | GLY112 |
| J | VAL113 |
| J | ALA215 |
| J | VAL217 |
| J | SER257 |
| J | ALA258 |
| J | GLY259 |
| J | VAL380 |
| J | TRP459 |
| J | HIS460 |
| J | ASP487 |
| J | GLY488 |
| J | HIS498 |
| J | PRO499 |
| J | GLN500 |
| site_id | BC2 |
| Number of Residues | 27 |
| Details | BINDING SITE FOR RESIDUE FAD K 773 |
| Chain | Residue |
| K | GLY33 |
| K | GLY35 |
| K | THR36 |
| K | SER37 |
| K | GLU55 |
| K | ARG56 |
| K | VAL98 |
| K | GLY100 |
| K | ARG101 |
| K | VAL102 |
| K | GLY105 |
| K | THR106 |
| K | SER107 |
| K | ASN110 |
| K | ALA111 |
| K | GLY112 |
| K | VAL113 |
| K | ALA215 |
| K | VAL217 |
| K | ALA258 |
| K | TRP459 |
| K | HIS460 |
| K | ASP487 |
| K | GLY488 |
| K | HIS498 |
| K | PRO499 |
| K | GLN500 |
| site_id | BC3 |
| Number of Residues | 30 |
| Details | BINDING SITE FOR RESIDUE FAD L 773 |
| Chain | Residue |
| L | GLY33 |
| L | GLY35 |
| L | THR36 |
| L | SER37 |
| L | GLU55 |
| L | ARG56 |
| L | VAL98 |
| L | GLY100 |
| L | ARG101 |
| L | VAL102 |
| L | GLY105 |
| L | THR106 |
| L | SER107 |
| L | ASN110 |
| L | ALA111 |
| L | GLY112 |
| L | VAL113 |
| L | ALA215 |
| L | VAL217 |
| L | SER257 |
| L | ALA258 |
| L | GLY259 |
| L | PRO260 |
| L | TRP459 |
| L | HIS460 |
| L | GLY488 |
| L | HIS498 |
| L | PRO499 |
| L | GLN500 |
| L | TYR503 |
Functional Information from PROSITE/UniProt
