6UHX
Crystal structure of YIR035C short chain dehydrogenases/reductase from Saccharomyces cerevisiae
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005737 | cellular_component | cytoplasm |
A | 0008150 | biological_process | biological_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 | 0050664 | molecular_function | oxidoreductase activity, acting on NAD(P)H, oxygen as acceptor |
A | 0102306 | molecular_function | benzil reductase [(S)-benzoin-forming] activity |
B | 0005737 | cellular_component | cytoplasm |
B | 0008150 | biological_process | biological_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 | 0050664 | molecular_function | oxidoreductase activity, acting on NAD(P)H, oxygen as acceptor |
B | 0102306 | molecular_function | benzil reductase [(S)-benzoin-forming] activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 23 |
Details | binding site for residue NAP A 301 |
Chain | Residue |
A | GLY9 |
A | ASN85 |
A | ALA86 |
A | GLY87 |
A | ILE109 |
A | SER136 |
A | SER137 |
A | TYR150 |
A | LYS154 |
A | PRO178 |
A | GLY179 |
A | SER11 |
A | VAL181 |
A | THR183 |
A | MET185 |
A | GLN186 |
A | ARG12 |
A | ILE14 |
A | ARG36 |
A | SER37 |
A | GLY57 |
A | ASP58 |
A | ILE59 |
site_id | AC2 |
Number of Residues | 26 |
Details | binding site for residue NAP B 301 |
Chain | Residue |
B | GLY9 |
B | SER11 |
B | ARG12 |
B | GLY13 |
B | ILE14 |
B | ALA35 |
B | ARG36 |
B | SER37 |
B | ASP58 |
B | ILE59 |
B | ASN85 |
B | ALA86 |
B | GLY87 |
B | VAL135 |
B | SER136 |
B | SER137 |
B | TYR150 |
B | LYS154 |
B | PRO178 |
B | GLY179 |
B | VAL181 |
B | THR183 |
B | ASP184 |
B | MET185 |
B | GLN186 |
B | HOH421 |
Functional Information from PROSITE/UniProt
site_id | PS00061 |
Number of Residues | 29 |
Details | ADH_SHORT Short-chain dehydrogenases/reductases family signature. SdacnmyfssWgaYGSSKAALnHFAmTLA |
Chain | Residue | Details |
A | SER137-ALA165 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | ACT_SITE: Proton donor => ECO:0000250|UniProtKB:O93868 |
Chain | Residue | Details |
A | SER136 | |
B | SER136 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU10001 |
Chain | Residue | Details |
A | TYR150 | |
B | TYR150 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | ACT_SITE: Lowers pKa of active site Tyr => ECO:0000250|UniProtKB:O93868 |
Chain | Residue | Details |
A | LYS154 | |
B | LYS154 |
site_id | SWS_FT_FI4 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000250|UniProtKB:L0E2Z4 |
Chain | Residue | Details |
A | VAL7 | |
A | THR183 | |
B | VAL7 | |
B | THR183 |
site_id | SWS_FT_FI5 |
Number of Residues | 8 |
Details | BINDING: BINDING => ECO:0000250|UniProtKB:O93868 |
Chain | Residue | Details |
A | ASN85 | |
A | TYR150 | |
A | LYS154 | |
A | VAL181 | |
B | ASN85 | |
B | TYR150 | |
B | LYS154 | |
B | VAL181 |