4R1S
Crystal structure of Petunia hydrida cinnamoyl-CoA reductase
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000166 | molecular_function | nucleotide binding |
A | 0005737 | cellular_component | cytoplasm |
A | 0007623 | biological_process | circadian rhythm |
A | 0009699 | biological_process | phenylpropanoid biosynthetic process |
A | 0009809 | biological_process | lignin biosynthetic process |
A | 0010597 | biological_process | green leaf volatile biosynthetic process |
A | 0016491 | molecular_function | oxidoreductase activity |
A | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
A | 0016621 | molecular_function | cinnamoyl-CoA reductase activity |
B | 0000166 | molecular_function | nucleotide binding |
B | 0005737 | cellular_component | cytoplasm |
B | 0007623 | biological_process | circadian rhythm |
B | 0009699 | biological_process | phenylpropanoid biosynthetic process |
B | 0009809 | biological_process | lignin biosynthetic process |
B | 0010597 | biological_process | green leaf volatile biosynthetic process |
B | 0016491 | molecular_function | oxidoreductase activity |
B | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
B | 0016621 | molecular_function | cinnamoyl-CoA reductase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 37 |
Details | BINDING SITE FOR RESIDUE NAP A 401 |
Chain | Residue |
A | GLY16 |
A | SER86 |
A | PRO87 |
A | THR121 |
A | SER122 |
A | TYR157 |
A | LYS161 |
A | PRO184 |
A | VAL185 |
A | LEU186 |
A | VAL187 |
A | PHE17 |
A | ASN197 |
A | SER199 |
A | HOH501 |
A | HOH504 |
A | HOH505 |
A | HOH507 |
A | HOH508 |
A | HOH510 |
A | HOH529 |
A | HOH538 |
A | ILE18 |
A | HOH572 |
A | HOH579 |
A | HOH581 |
A | HOH615 |
A | HOH630 |
A | HOH655 |
A | HOH692 |
A | HOH706 |
A | ARG38 |
A | LYS44 |
A | ASP64 |
A | LEU65 |
A | THR84 |
A | ALA85 |
site_id | AC2 |
Number of Residues | 34 |
Details | BINDING SITE FOR RESIDUE NAP B 401 |
Chain | Residue |
B | GLY16 |
B | PHE17 |
B | ILE18 |
B | ARG38 |
B | LYS44 |
B | ASP64 |
B | LEU65 |
B | THR84 |
B | ALA85 |
B | SER86 |
B | PRO87 |
B | THR121 |
B | SER122 |
B | TYR157 |
B | LYS161 |
B | PRO184 |
B | VAL185 |
B | VAL187 |
B | SER199 |
B | HOH502 |
B | HOH503 |
B | HOH504 |
B | HOH507 |
B | HOH508 |
B | HOH512 |
B | HOH526 |
B | HOH547 |
B | HOH564 |
B | HOH570 |
B | HOH600 |
B | HOH606 |
B | HOH608 |
B | HOH644 |
B | HOH685 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | ACT_SITE: Proton donor => ECO:0000250|UniProtKB:Q12068 |
Chain | Residue | Details |
A | LYS161 | |
B | LYS161 |
site_id | SWS_FT_FI2 |
Number of Residues | 18 |
Details | BINDING: BINDING => ECO:0000269|PubMed:25217505, ECO:0007744|PDB:4R1S |
Chain | Residue | Details |
A | GLY13 | |
B | GLY13 | |
B | ARG38 | |
B | LYS44 | |
B | ASP64 | |
B | THR84 | |
B | TYR157 | |
B | LYS161 | |
B | PRO184 | |
B | SER199 | |
A | ARG38 | |
A | LYS44 | |
A | ASP64 | |
A | THR84 | |
A | TYR157 | |
A | LYS161 | |
A | PRO184 | |
A | SER199 |