1Q7C
The structure of betaketoacyl-[ACP] reductase Y151F mutant in complex with NADPH fragment
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004316 | molecular_function | 3-oxoacyl-[acyl-carrier-protein] reductase (NADPH) activity |
| A | 0005829 | cellular_component | cytosol |
| A | 0006633 | biological_process | fatty acid biosynthetic process |
| A | 0008610 | biological_process | lipid biosynthetic process |
| A | 0009102 | biological_process | biotin biosynthetic process |
| 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 | 0030497 | biological_process | fatty acid elongation |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0050661 | molecular_function | NADP binding |
| A | 0051287 | molecular_function | NAD binding |
| B | 0004316 | molecular_function | 3-oxoacyl-[acyl-carrier-protein] reductase (NADPH) activity |
| B | 0005829 | cellular_component | cytosol |
| B | 0006633 | biological_process | fatty acid biosynthetic process |
| B | 0008610 | biological_process | lipid biosynthetic process |
| B | 0009102 | biological_process | biotin biosynthetic process |
| 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 | 0030497 | biological_process | fatty acid elongation |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0050661 | molecular_function | NADP binding |
| B | 0051287 | molecular_function | NAD binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE NDP A 1901 |
| Chain | Residue |
| A | GLY12 |
| A | GLY88 |
| A | ILE89 |
| A | ARG91 |
| A | HOH1011 |
| A | SER14 |
| A | ARG15 |
| A | ALA36 |
| A | THR37 |
| A | LEU58 |
| A | ASN59 |
| A | VAL60 |
| A | ALA87 |
| site_id | AC2 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE NDP B 2901 |
| Chain | Residue |
| B | SER14 |
| B | ALA36 |
| B | THR37 |
| B | LEU58 |
| B | ASN59 |
| B | VAL60 |
| B | ALA87 |
| B | GLY88 |
| B | ILE89 |
| B | ARG91 |
| B | HOH2011 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU10001 |
| Chain | Residue | Details |
| A | PHE151 | |
| B | PHE151 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:15016358, ECO:0007744|PDB:1Q7B, ECO:0007744|PDB:1Q7C |
| Chain | Residue | Details |
| A | GLY12 | |
| A | THR37 | |
| A | ASN59 | |
| A | PHE151 | |
| B | GLY12 | |
| B | THR37 | |
| B | ASN59 | |
| B | PHE151 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 10 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | GLY50 | |
| B | THR234 | |
| A | GLY53 | |
| A | ASN145 | |
| A | GLU233 | |
| A | THR234 | |
| B | GLY50 | |
| B | GLY53 | |
| B | ASN145 | |
| B | GLU233 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:15016358, ECO:0007744|PDB:1Q7B |
| Chain | Residue | Details |
| A | ASN86 | |
| B | ASN86 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000250 |
| Chain | Residue | Details |
| A | SER138 | |
| B | SER138 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:15016358 |
| Chain | Residue | Details |
| A | ILE184 | |
| B | ILE184 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1ybv |
| Chain | Residue | Details |
| A | LYS155 | |
| A | SER138 | |
| A | PHE151 | |
| A | ASN110 |
| site_id | CSA2 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1ybv |
| Chain | Residue | Details |
| B | LYS155 | |
| B | SER138 | |
| B | PHE151 | |
| B | ASN110 |
| site_id | CSA3 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ybv |
| Chain | Residue | Details |
| A | LYS155 | |
| A | GLN148 |
| site_id | CSA4 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ybv |
| Chain | Residue | Details |
| B | LYS155 | |
| B | GLN148 |
| site_id | CSA5 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ybv |
| Chain | Residue | Details |
| A | LYS155 | |
| A | PHE151 |
| site_id | CSA6 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ybv |
| Chain | Residue | Details |
| B | LYS155 | |
| B | PHE151 |
