1PR9
Human L-Xylulose Reductase Holoenzyme
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 | 0005739 | cellular_component | mitochondrion |
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 | 0005739 | cellular_component | mitochondrion |
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 | 1 |
Details | BINDING SITE FOR RESIDUE K A 246 |
Chain | Residue |
A | 2HP247 |
site_id | AC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE K B 1246 |
Chain | Residue |
B | TYR149 |
B | HOH459 |
B | HOH462 |
B | 2HP1247 |
site_id | AC3 |
Number of Residues | 32 |
Details | BINDING SITE FOR RESIDUE NAP A 245 |
Chain | Residue |
A | ILE19 |
A | SER38 |
A | ARG39 |
A | THR40 |
A | ASP43 |
A | VAL59 |
A | ASP60 |
A | LEU61 |
A | GLY62 |
A | ASN83 |
A | ALA85 |
A | ARG102 |
A | VAL134 |
A | SER135 |
A | TYR149 |
A | LYS153 |
A | PRO179 |
A | THR180 |
A | VAL181 |
A | VAL182 |
A | THR184 |
A | SER185 |
A | MET186 |
A | HOH302 |
A | HOH308 |
A | HOH413 |
A | HOH445 |
A | HOH451 |
A | GLY14 |
A | GLY16 |
A | LYS17 |
A | GLY18 |
site_id | AC4 |
Number of Residues | 35 |
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 | VAL59 |
B | ASP60 |
B | LEU61 |
B | GLY62 |
B | ASN83 |
B | ALA85 |
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 | MET186 |
B | GLY187 |
B | HOH359 |
B | HOH360 |
B | HOH383 |
B | HOH401 |
B | HOH443 |
B | HOH462 |
B | 2HP1247 |
site_id | AC5 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE 2HP A 247 |
Chain | Residue |
A | SER136 |
A | CYS138 |
A | HIS146 |
A | TYR149 |
A | VAL181 |
A | TRP191 |
A | K246 |
site_id | AC6 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE 2HP B 1247 |
Chain | Residue |
B | SER136 |
B | CYS138 |
B | VAL143 |
B | HIS146 |
B | VAL181 |
B | MET200 |
B | HOH459 |
B | NAP1245 |
B | K1246 |
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 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | ACT_SITE: Proton acceptor |
Chain | Residue | Details |
A | TYR149 | |
B | TYR149 |
site_id | SWS_FT_FI2 |
Number of Residues | 6 |
Details | BINDING: BINDING => ECO:0000269|PubMed:15103634 |
Chain | Residue | Details |
A | LEU11 | |
A | SER136 | |
A | LYS153 | |
B | LEU11 | |
B | SER136 | |
B | LYS153 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | MOD_RES: N-acetylmethionine => ECO:0000269|PubMed:12665801, ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378, ECO:0007744|PubMed:25944712 |
Chain | Residue | Details |
A | MET1 | |
B | MET1 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | MOD_RES: Omega-N-methylarginine => ECO:0007744|PubMed:24129315 |
Chain | Residue | Details |
A | ARG21 | |
B | ARG21 |
site_id | SWS_FT_FI5 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:24275569 |
Chain | Residue | Details |
A | SER46 | |
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 |