1MZR
Structure of dkga from E.coli at 2.13 A resolution solved by molecular replacement
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004032 | molecular_function | aldose reductase (NADPH) activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0008106 | molecular_function | alcohol dehydrogenase (NADP+) activity |
| 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 | 0050580 | molecular_function | 2,5-didehydrogluconate reductase activity |
| A | 0051596 | biological_process | methylglyoxal catabolic process |
| A | 1990002 | molecular_function | methylglyoxal reductase (NADPH) (acetol producing) activity |
| B | 0004032 | molecular_function | aldose reductase (NADPH) activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0008106 | molecular_function | alcohol dehydrogenase (NADP+) activity |
| 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 | 0050580 | molecular_function | 2,5-didehydrogluconate reductase activity |
| B | 0051596 | biological_process | methylglyoxal catabolic process |
| B | 1990002 | molecular_function | methylglyoxal reductase (NADPH) (acetol producing) activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE PO4 A 900 |
| Chain | Residue |
| A | SER188 |
| A | PRO189 |
| A | LEU190 |
| A | PRO231 |
| A | LYS232 |
| A | HOH667 |
| A | HOH677 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE PO4 A 901 |
| Chain | Residue |
| A | THR235 |
| A | ARG238 |
| A | SER233 |
| A | VAL234 |
| site_id | AC3 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE PO4 B 902 |
| Chain | Residue |
| B | SER188 |
| B | PRO189 |
| B | LEU190 |
| B | ALA191 |
| B | PRO231 |
| B | LYS232 |
| B | HOH639 |
| B | HOH770 |
| site_id | AC4 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE PO4 B 904 |
| Chain | Residue |
| A | ARG171 |
| A | GLN172 |
| A | ASP262 |
| A | HOH363 |
| B | ARG171 |
| B | GLN172 |
| B | ASP262 |
| B | HOH316 |
| B | HOH398 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE PO4 B 905 |
| Chain | Residue |
| B | LYS84 |
| B | ARG85 |
| B | PRO86 |
| B | ARG87 |
| B | HOH325 |
| B | HOH412 |
| B | HOH476 |
| site_id | AC6 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL A 910 |
| Chain | Residue |
| A | TRP24 |
| A | TYR52 |
| A | TRP79 |
| A | HIS108 |
| A | TRP109 |
| A | HOH497 |
| A | GOL911 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE GOL A 911 |
| Chain | Residue |
| A | GLN25 |
| A | TRP79 |
| A | GOL910 |
Functional Information from PROSITE/UniProt
| site_id | PS00062 |
| Number of Residues | 18 |
| Details | ALDOKETO_REDUCTASE_2 Aldo/keto reductase family signature 2. MielqkeglIKSIGVCNF |
| Chain | Residue | Details |
| A | MET124-PHE141 |
| site_id | PS00063 |
| Number of Residues | 16 |
| Details | ALDOKETO_REDUCTASE_3 Aldo/keto reductase family putative active site signature. IPKSVTpsRIaENfDV |
| Chain | Residue | Details |
| A | ILE230-VAL245 |
| site_id | PS00798 |
| Number of Residues | 18 |
| Details | ALDOKETO_REDUCTASE_1 Aldo/keto reductase family signature 1. GYRSIDTAaayknEegVG |
| Chain | Residue | Details |
| A | GLY42-GLY59 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton donor","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 110 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1mrq |
| Chain | Residue | Details |
| A | ASP47 | |
| A | TYR52 | |
| A | LYS77 | |
| A | HIS108 |
| site_id | CSA2 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1mrq |
| Chain | Residue | Details |
| B | ASP47 | |
| B | TYR52 | |
| B | LYS77 | |
| B | HIS108 |
| site_id | CSA3 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1mrq |
| Chain | Residue | Details |
| A | TYR52 | |
| A | LYS77 |
| site_id | CSA4 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1mrq |
| Chain | Residue | Details |
| B | TYR52 | |
| B | LYS77 |
