3D3W
Structure of L-Xylulose Reductase with bound coenzyme, phosphate and hydroxide.
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004090 | molecular_function | carbonyl reductase (NADPH) activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005634 | cellular_component | nucleus |
| A | 0005829 | cellular_component | cytosol |
| A | 0005881 | cellular_component | cytoplasmic microtubule |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0005902 | cellular_component | microvillus |
| A | 0005903 | cellular_component | brush border |
| A | 0005997 | biological_process | xylulose metabolic process |
| A | 0006006 | biological_process | glucose metabolic process |
| A | 0006739 | biological_process | NADP metabolic process |
| A | 0016020 | cellular_component | membrane |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016614 | molecular_function | oxidoreductase activity, acting on CH-OH group of donors |
| A | 0016655 | molecular_function | oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor |
| A | 0019640 | biological_process | glucuronate catabolic process to xylulose 5-phosphate |
| A | 0042732 | biological_process | D-xylose metabolic process |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0050038 | molecular_function | L-xylulose reductase (NADPH) activity |
| A | 0070062 | cellular_component | extracellular exosome |
| A | 2000379 | biological_process | positive regulation of reactive oxygen species metabolic process |
| B | 0004090 | molecular_function | carbonyl reductase (NADPH) activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0005634 | cellular_component | nucleus |
| B | 0005829 | cellular_component | cytosol |
| B | 0005881 | cellular_component | cytoplasmic microtubule |
| B | 0005886 | cellular_component | plasma membrane |
| B | 0005902 | cellular_component | microvillus |
| B | 0005903 | cellular_component | brush border |
| B | 0005997 | biological_process | xylulose metabolic process |
| B | 0006006 | biological_process | glucose metabolic process |
| B | 0006739 | biological_process | NADP metabolic process |
| B | 0016020 | cellular_component | membrane |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0016614 | molecular_function | oxidoreductase activity, acting on CH-OH group of donors |
| B | 0016655 | molecular_function | oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor |
| B | 0019640 | biological_process | glucuronate catabolic process to xylulose 5-phosphate |
| B | 0042732 | biological_process | D-xylose metabolic process |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0050038 | molecular_function | L-xylulose reductase (NADPH) activity |
| B | 0070062 | cellular_component | extracellular exosome |
| B | 2000379 | biological_process | positive regulation of reactive oxygen species metabolic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 37 |
| Details | BINDING SITE FOR RESIDUE NAP A 245 |
| Chain | Residue |
| A | GLY14 |
| A | VAL59 |
| A | ASP60 |
| A | LEU61 |
| A | GLY62 |
| A | ASN83 |
| A | ALA84 |
| A | ALA85 |
| A | VAL86 |
| A | ARG102 |
| A | VAL106 |
| A | GLY16 |
| A | VAL134 |
| A | SER135 |
| A | SER136 |
| A | TYR149 |
| A | LYS153 |
| A | PRO179 |
| A | THR180 |
| A | VAL182 |
| A | THR184 |
| A | SER185 |
| A | LYS17 |
| A | MET186 |
| A | GLY187 |
| A | HOH259 |
| A | HOH263 |
| A | HOH270 |
| A | HOH295 |
| A | HOH297 |
| A | HOH367 |
| A | GLY18 |
| A | ILE19 |
| A | SER38 |
| A | ARG39 |
| A | THR40 |
| A | ASP43 |
| site_id | AC2 |
| Number of Residues | 39 |
| Details | BINDING SITE FOR RESIDUE NAP B 1245 |
| Chain | Residue |
| B | GLY14 |
| B | GLY16 |
| B | LYS17 |
| B | GLY18 |
| B | ILE19 |
| B | SER38 |
| B | ARG39 |
| B | THR40 |
| B | ASP43 |
| B | VAL59 |
| B | ASP60 |
| B | LEU61 |
| B | GLY62 |
| B | ASN83 |
| B | ALA84 |
| B | ALA85 |
| B | ARG102 |
| B | VAL106 |
| B | VAL134 |
| B | SER135 |
| B | SER136 |
| B | TYR149 |
| B | LYS153 |
| B | PRO179 |
| B | THR180 |
| B | VAL181 |
| B | VAL182 |
| B | THR184 |
| B | SER185 |
| B | GLY187 |
| B | PO4245 |
| B | HOH1250 |
| B | HOH1281 |
| B | HOH1307 |
| B | HOH1319 |
| B | HOH1345 |
| B | HOH1362 |
| B | HOH1410 |
| B | HOH1439 |
| site_id | AC3 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE PO4 B 245 |
| Chain | Residue |
| B | SER136 |
| B | GLN137 |
| B | CYS138 |
| B | PRO179 |
| B | THR180 |
| B | VAL181 |
| B | MET200 |
| B | NAP1245 |
| B | HOH1439 |
Functional Information from PROSITE/UniProt
| site_id | PS00061 |
| Number of Residues | 29 |
| Details | ADH_SHORT Short-chain dehydrogenases/reductases family signature. SqcsqravtnHsvYCSTKGALdMLTkVMA |
| Chain | Residue | Details |
| A | SER136-ALA164 | |
| B | SER136-ALA164 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | ACT_SITE: Proton acceptor |
| Chain | Residue | Details |
| B | TYR149 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 3 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:15103634 |
| Chain | Residue | Details |
| B | LEU11 | |
| B | SER136 | |
| B | LYS153 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | MOD_RES: N-acetylmethionine => ECO:0000269|PubMed:12665801, ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378, ECO:0007744|PubMed:25944712 |
| Chain | Residue | Details |
| B | MET1 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | MOD_RES: Omega-N-methylarginine => ECO:0007744|PubMed:24129315 |
| Chain | Residue | Details |
| B | ARG21 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:24275569 |
| Chain | Residue | Details |
| B | SER46 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| A | SER136 | |
| A | TYR149 | |
| A | LYS153 |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| B | SER136 | |
| B | TYR149 | |
| B | LYS153 |
| site_id | CSA3 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| A | SER136 | |
| A | ASN107 | |
| A | TYR149 | |
| A | LYS153 |
| site_id | CSA4 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| B | SER136 | |
| B | ASN107 | |
| B | TYR149 | |
| B | LYS153 |
| site_id | CSA5 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| A | HIS146 | |
| A | LYS153 |
| site_id | CSA6 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| B | HIS146 | |
| B | LYS153 |
| site_id | CSA7 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| A | TYR149 | |
| A | LYS153 |
| site_id | CSA8 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| B | TYR149 | |
| B | LYS153 |
