1MI3
1.8 Angstrom structure of xylose reductase from Candida tenuis in complex with NAD
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004032 | molecular_function | aldose reductase (NADPH) activity |
| A | 0005829 | cellular_component | cytosol |
| 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 | 0032866 | molecular_function | D-xylose reductase (NADPH) activity |
| A | 0042732 | biological_process | D-xylose metabolic process |
| A | 0042843 | biological_process | D-xylose catabolic process |
| B | 0004032 | molecular_function | aldose reductase (NADPH) activity |
| B | 0005829 | cellular_component | cytosol |
| 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 | 0032866 | molecular_function | D-xylose reductase (NADPH) activity |
| B | 0042732 | biological_process | D-xylose metabolic process |
| B | 0042843 | biological_process | D-xylose catabolic process |
| C | 0004032 | molecular_function | aldose reductase (NADPH) activity |
| C | 0005829 | cellular_component | cytosol |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
| C | 0032866 | molecular_function | D-xylose reductase (NADPH) activity |
| C | 0042732 | biological_process | D-xylose metabolic process |
| C | 0042843 | biological_process | D-xylose catabolic process |
| D | 0004032 | molecular_function | aldose reductase (NADPH) activity |
| D | 0005829 | cellular_component | cytosol |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
| D | 0032866 | molecular_function | D-xylose reductase (NADPH) activity |
| D | 0042732 | biological_process | D-xylose metabolic process |
| D | 0042843 | biological_process | D-xylose catabolic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 28 |
| Details | BINDING SITE FOR RESIDUE NAD A 1350 |
| Chain | Residue |
| A | GLY22 |
| A | GLN191 |
| A | TYR217 |
| A | SER218 |
| A | SER219 |
| A | PHE220 |
| A | GLN223 |
| A | SER224 |
| A | GLU227 |
| A | ALA257 |
| A | ILE272 |
| A | CYS23 |
| A | PRO273 |
| A | LYS274 |
| A | ASN276 |
| A | ARG280 |
| A | ASN284 |
| A | ASN310 |
| A | HOH1404 |
| A | HOH1411 |
| A | HOH1453 |
| A | TRP24 |
| A | ASP47 |
| A | TYR52 |
| A | LYS81 |
| A | HIS114 |
| A | SER169 |
| A | ASN170 |
| site_id | AC2 |
| Number of Residues | 32 |
| Details | BINDING SITE FOR RESIDUE NAD B 2350 |
| Chain | Residue |
| B | GLY22 |
| B | CYS23 |
| B | TRP24 |
| B | ASP47 |
| B | TYR52 |
| B | LYS81 |
| B | HIS114 |
| B | SER169 |
| B | ASN170 |
| B | GLN191 |
| B | TYR217 |
| B | SER218 |
| B | SER219 |
| B | PHE220 |
| B | GLN223 |
| B | SER224 |
| B | GLU227 |
| B | ASN229 |
| B | PHE240 |
| B | ALA257 |
| B | ILE272 |
| B | PRO273 |
| B | LYS274 |
| B | ASN276 |
| B | ARG280 |
| B | GLN283 |
| B | ASN284 |
| B | ASN310 |
| B | HOH2352 |
| B | HOH2360 |
| B | HOH2435 |
| B | HOH2483 |
| site_id | AC3 |
| Number of Residues | 28 |
| Details | BINDING SITE FOR RESIDUE NAD C 3350 |
| Chain | Residue |
| C | GLY22 |
| C | CYS23 |
| C | TRP24 |
| C | ASP47 |
| C | TYR52 |
| C | LYS81 |
| C | HIS114 |
| C | SER169 |
| C | ASN170 |
| C | GLN191 |
| C | TYR217 |
| C | SER218 |
| C | SER219 |
| C | PHE220 |
| C | GLN223 |
| C | SER224 |
| C | GLU227 |
| C | ALA257 |
| C | ILE272 |
| C | PRO273 |
| C | LYS274 |
| C | ASN276 |
| C | ARG280 |
| C | GLN283 |
| C | ASN284 |
| C | ASN310 |
| C | HOH3404 |
| C | HOH3465 |
| site_id | AC4 |
| Number of Residues | 32 |
| Details | BINDING SITE FOR RESIDUE NAD D 4350 |
| Chain | Residue |
| D | SER218 |
| D | SER219 |
| D | PHE220 |
| D | GLN223 |
| D | SER224 |
| D | GLU227 |
| D | ASN229 |
| D | PHE240 |
| D | ALA257 |
| D | ILE272 |
| D | PRO273 |
| D | LYS274 |
| D | ASN276 |
| D | ARG280 |
| D | GLN283 |
| D | ASN284 |
| D | ASN310 |
| D | HOH4358 |
| D | HOH4374 |
| D | HOH4465 |
| D | HOH4572 |
| D | GLY22 |
| D | CYS23 |
| D | TRP24 |
| D | ASP47 |
| D | TYR52 |
| D | LYS81 |
| D | HIS114 |
| D | SER169 |
| D | ASN170 |
| D | GLN191 |
| D | TYR217 |
Functional Information from PROSITE/UniProt
| site_id | PS00062 |
| Number of Residues | 18 |
| Details | ALDOKETO_REDUCTASE_2 Aldo/keto reductase family signature 2. LeklvaagkIKSIGVSNF |
| Chain | Residue | Details |
| A | LEU154-PHE171 |
| site_id | PS00063 |
| Number of Residues | 16 |
| Details | ALDOKETO_REDUCTASE_3 Aldo/keto reductase family putative active site signature. IPKSNLpeRLvQNrSF |
| Chain | Residue | Details |
| A | ILE272-PHE287 |
| site_id | PS00798 |
| Number of Residues | 18 |
| Details | ALDOKETO_REDUCTASE_1 Aldo/keto reductase family signature 1. GYRLFDGAedygnEkeVG |
| Chain | Residue | Details |
| A | GLY42-GLY59 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | ACT_SITE: Proton donor |
| Chain | Residue | Details |
| A | TYR52 | |
| B | TYR52 | |
| C | TYR52 | |
| D | TYR52 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000250 |
| Chain | Residue | Details |
| A | HIS114 | |
| B | HIS114 | |
| C | HIS114 | |
| D | HIS114 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 12 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:12733986, ECO:0000269|PubMed:15320875, ECO:0000269|PubMed:16336198 |
| Chain | Residue | Details |
| A | SER169 | |
| D | SER169 | |
| D | SER218 | |
| D | LYS274 | |
| A | SER218 | |
| A | LYS274 | |
| B | SER169 | |
| B | SER218 | |
| B | LYS274 | |
| C | SER169 | |
| C | SER218 | |
| C | LYS274 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | SITE: Lowers pKa of active site Tyr => ECO:0000250 |
| Chain | Residue | Details |
| A | LYS81 | |
| B | LYS81 | |
| C | LYS81 | |
| D | LYS81 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1mrq |
| Chain | Residue | Details |
| A | LYS81 | |
| A | ASP47 | |
| A | HIS114 | |
| A | TYR52 |
| site_id | CSA2 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1mrq |
| Chain | Residue | Details |
| B | LYS81 | |
| B | ASP47 | |
| B | HIS114 | |
| B | TYR52 |
| site_id | CSA3 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1mrq |
| Chain | Residue | Details |
| C | LYS81 | |
| C | ASP47 | |
| C | HIS114 | |
| C | TYR52 |
| site_id | CSA4 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1mrq |
| Chain | Residue | Details |
| D | LYS81 | |
| D | ASP47 | |
| D | HIS114 | |
| D | TYR52 |
| site_id | CSA5 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1mrq |
| Chain | Residue | Details |
| A | LYS81 | |
| A | TYR52 |
| site_id | CSA6 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1mrq |
| Chain | Residue | Details |
| B | LYS81 | |
| B | TYR52 |
| site_id | CSA7 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1mrq |
| Chain | Residue | Details |
| C | LYS81 | |
| C | TYR52 |
| site_id | CSA8 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1mrq |
| Chain | Residue | Details |
| D | LYS81 | |
| D | TYR52 |
