Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005737 | cellular_component | cytoplasm |
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 | 0019853 | biological_process | L-ascorbic acid biosynthetic process |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 31 |
Details | BINDING SITE FOR RESIDUE NDP A 300 |
Chain | Residue |
A | GLY20 |
A | VAL21 |
A | PHE22 |
A | ASP45 |
A | TYR50 |
A | LYS75 |
A | HIS108 |
A | SER139 |
A | ASN140 |
A | GLN161 |
A | TRP187 |
A | GLY188 |
A | PRO189 |
A | LEU190 |
A | GLY191 |
A | GLN192 |
A | ALA215 |
A | PHE230 |
A | PRO231 |
A | LYS232 |
A | SER233 |
A | VAL234 |
A | ARG235 |
A | ARG238 |
A | GLU241 |
A | ASN242 |
A | HOH332 |
A | HOH342 |
A | HOH352 |
A | HOH396 |
A | HOH406 |
site_id | CIC |
Number of Residues | 9 |
Details | THE RESIDUE LINE THE ACTIVE SITE OF THE ENZYME. |
Chain | Residue |
A | PHE22 |
A | ASP45 |
A | ALA47 |
A | TYR50 |
A | LYS75 |
A | LEU106 |
A | SER139 |
A | ASN140 |
A | TRP187 |
Functional Information from PROSITE/UniProt
site_id | PS00798 |
Number of Residues | 18 |
Details | ALDOKETO_REDUCTASE_1 Aldo/keto reductase family signature 1. GYRHIDTAaiygnEegVG |
Chain | Residue | Details |
A | GLY40-GLY57 | |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
A | TYR50 | |
Chain | Residue | Details |
A | HIS108 | |
Chain | Residue | Details |
A | GLY188 | |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1mrq |
Chain | Residue | Details |
A | LYS75 | |
A | ASP45 | |
A | TYR50 | |
A | HIS108 | |
site_id | CSA2 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1mrq |
Chain | Residue | Details |
A | LYS75 | |
A | TYR50 | |