1CYD
CARBONYL REDUCTASE COMPLEXED WITH NADPH AND 2-PROPANOL
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004090 | molecular_function | carbonyl reductase (NADPH) activity |
A | 0005515 | molecular_function | protein binding |
A | 0005739 | cellular_component | mitochondrion |
A | 0005759 | cellular_component | mitochondrial matrix |
A | 0006116 | biological_process | NADH oxidation |
A | 0016491 | molecular_function | oxidoreductase activity |
A | 0042802 | molecular_function | identical protein binding |
A | 0044281 | biological_process | small molecule metabolic process |
B | 0004090 | molecular_function | carbonyl reductase (NADPH) activity |
B | 0005515 | molecular_function | protein binding |
B | 0005739 | cellular_component | mitochondrion |
B | 0005759 | cellular_component | mitochondrial matrix |
B | 0006116 | biological_process | NADH oxidation |
B | 0016491 | molecular_function | oxidoreductase activity |
B | 0042802 | molecular_function | identical protein binding |
B | 0044281 | biological_process | small molecule metabolic process |
C | 0004090 | molecular_function | carbonyl reductase (NADPH) activity |
C | 0005515 | molecular_function | protein binding |
C | 0005739 | cellular_component | mitochondrion |
C | 0005759 | cellular_component | mitochondrial matrix |
C | 0006116 | biological_process | NADH oxidation |
C | 0016491 | molecular_function | oxidoreductase activity |
C | 0042802 | molecular_function | identical protein binding |
C | 0044281 | biological_process | small molecule metabolic process |
D | 0004090 | molecular_function | carbonyl reductase (NADPH) activity |
D | 0005515 | molecular_function | protein binding |
D | 0005739 | cellular_component | mitochondrion |
D | 0005759 | cellular_component | mitochondrial matrix |
D | 0006116 | biological_process | NADH oxidation |
D | 0016491 | molecular_function | oxidoreductase activity |
D | 0042802 | molecular_function | identical protein binding |
D | 0044281 | biological_process | small molecule metabolic process |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 35 |
Details | BINDING SITE FOR RESIDUE NDP A 245 |
Chain | Residue |
A | GLY14 |
A | ASP60 |
A | LEU61 |
A | ASN83 |
A | ALA85 |
A | ARG102 |
A | VAL106 |
A | VAL134 |
A | SER135 |
A | SER136 |
A | TYR149 |
A | GLY16 |
A | LYS153 |
A | PRO179 |
A | THR180 |
A | VAL181 |
A | VAL182 |
A | THR184 |
A | MET186 |
A | GLY187 |
A | IPA246 |
A | HOH250 |
A | LYS17 |
A | HOH283 |
A | HOH284 |
A | HOH302 |
A | HOH311 |
A | HOH347 |
A | HOH361 |
A | GLY18 |
A | ILE19 |
A | THR38 |
A | ARG39 |
A | THR40 |
A | VAL59 |
site_id | AC2 |
Number of Residues | 37 |
Details | BINDING SITE FOR RESIDUE NDP B 245 |
Chain | Residue |
B | GLY14 |
B | GLY16 |
B | LYS17 |
B | GLY18 |
B | ILE19 |
B | THR38 |
B | ARG39 |
B | THR40 |
B | VAL59 |
B | ASP60 |
B | LEU61 |
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 | ASP185 |
B | MET186 |
B | GLY187 |
B | IPA246 |
B | HOH247 |
B | HOH273 |
B | HOH301 |
B | HOH314 |
B | HOH388 |
B | HOH391 |
B | HOH393 |
site_id | AC3 |
Number of Residues | 32 |
Details | BINDING SITE FOR RESIDUE NDP C 245 |
Chain | Residue |
C | HOH280 |
C | HOH285 |
C | HOH293 |
C | HOH305 |
C | HOH382 |
C | GLY14 |
C | GLY16 |
C | LYS17 |
C | GLY18 |
C | ILE19 |
C | THR38 |
C | ARG39 |
C | THR40 |
C | VAL59 |
C | ASP60 |
C | LEU61 |
C | ASN83 |
C | ALA85 |
C | VAL106 |
C | VAL134 |
C | SER135 |
C | TYR149 |
C | LYS153 |
C | PRO179 |
C | THR180 |
C | VAL181 |
C | VAL182 |
C | THR184 |
C | MET186 |
C | GLY187 |
C | IPA246 |
C | HOH248 |
site_id | AC4 |
Number of Residues | 33 |
Details | BINDING SITE FOR RESIDUE NDP D 245 |
Chain | Residue |
D | GLY14 |
D | GLY16 |
D | LYS17 |
D | GLY18 |
D | ILE19 |
D | THR38 |
D | ARG39 |
D | THR40 |
D | VAL59 |
D | ASP60 |
D | LEU61 |
D | ASN83 |
D | ALA85 |
D | VAL106 |
D | VAL134 |
D | SER135 |
D | SER136 |
D | TYR149 |
D | LYS153 |
D | PRO179 |
D | THR180 |
D | VAL181 |
D | VAL182 |
D | THR184 |
D | MET186 |
D | GLY187 |
D | IPA246 |
D | HOH248 |
D | HOH253 |
D | HOH340 |
D | HOH353 |
D | HOH364 |
D | HOH394 |
site_id | AC5 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE IPA A 246 |
Chain | Residue |
A | SER136 |
A | LEU146 |
A | TYR149 |
A | VAL190 |
A | NDP245 |
site_id | AC6 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE IPA B 246 |
Chain | Residue |
B | SER136 |
B | TYR149 |
B | NDP245 |
site_id | AC7 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE IPA C 246 |
Chain | Residue |
C | SER136 |
C | TYR149 |
C | NDP245 |
site_id | AC8 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE IPA D 246 |
Chain | Residue |
D | SER136 |
D | LEU146 |
D | TYR149 |
D | NDP245 |
Functional Information from PROSITE/UniProt
site_id | PS00061 |
Number of Residues | 29 |
Details | ADH_SHORT Short-chain dehydrogenases/reductases family signature. SmvahvtfpnLitYSSTKGAMtMLTkAMA |
Chain | Residue | Details |
A | SER136-ALA164 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 4 |
Details | ACT_SITE: Proton acceptor |
Chain | Residue | Details |
A | TYR149 | |
B | TYR149 | |
C | TYR149 | |
D | TYR149 |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000269|PubMed:8805511 |
Chain | Residue | Details |
A | LEU11 | |
B | LEU11 | |
C | LEU11 | |
D | LEU11 |
site_id | SWS_FT_FI3 |
Number of Residues | 4 |
Details | BINDING: |
Chain | Residue | Details |
A | SER136 | |
B | SER136 | |
C | SER136 | |
D | SER136 |
site_id | SWS_FT_FI4 |
Number of Residues | 8 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:21183079 |
Chain | Residue | Details |
A | SER42 | |
A | SER176 | |
B | SER42 | |
B | SER176 | |
C | SER42 | |
C | SER176 | |
D | SER42 | |
D | SER176 |
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 | CSA10 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1eq2 |
Chain | Residue | Details |
B | LEU146 | |
B | LYS153 |
site_id | CSA11 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1eq2 |
Chain | Residue | Details |
C | LEU146 | |
C | LYS153 |
site_id | CSA12 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1eq2 |
Chain | Residue | Details |
D | LEU146 | |
D | LYS153 |
site_id | CSA13 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1eq2 |
Chain | Residue | Details |
A | TYR149 | |
A | LYS153 |
site_id | CSA14 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1eq2 |
Chain | Residue | Details |
B | TYR149 | |
B | LYS153 |
site_id | CSA15 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1eq2 |
Chain | Residue | Details |
C | TYR149 | |
C | LYS153 |
site_id | CSA16 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1eq2 |
Chain | Residue | Details |
D | TYR149 | |
D | 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 | 3 |
Details | Annotated By Reference To The Literature 1eq2 |
Chain | Residue | Details |
C | SER136 | |
C | TYR149 | |
C | LYS153 |
site_id | CSA4 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1eq2 |
Chain | Residue | Details |
D | SER136 | |
D | TYR149 | |
D | LYS153 |
site_id | CSA5 |
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 | CSA6 |
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 | CSA7 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1eq2 |
Chain | Residue | Details |
C | SER136 | |
C | ASN107 | |
C | TYR149 | |
C | LYS153 |
site_id | CSA8 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1eq2 |
Chain | Residue | Details |
D | SER136 | |
D | ASN107 | |
D | TYR149 | |
D | LYS153 |
site_id | CSA9 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1eq2 |
Chain | Residue | Details |
A | LEU146 | |
A | LYS153 |