2PNF
Structure of Aquifex Aeolicus FabG 3-oxoacyl-(acyl-carrier protein) reductase
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004316 | molecular_function | 3-oxoacyl-[acyl-carrier-protein] reductase (NADPH) activity |
A | 0006629 | biological_process | lipid metabolic process |
A | 0006631 | biological_process | fatty acid metabolic process |
A | 0006633 | biological_process | fatty acid 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 | 0032787 | biological_process | monocarboxylic acid metabolic process |
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 | 0006629 | biological_process | lipid metabolic process |
B | 0006631 | biological_process | fatty acid metabolic process |
B | 0006633 | biological_process | fatty acid 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 | 0032787 | biological_process | monocarboxylic acid metabolic process |
B | 0050661 | molecular_function | NADP binding |
B | 0051287 | molecular_function | NAD binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE 1PE A 401 |
Chain | Residue |
A | LYS4 |
A | LEU5 |
A | GLN6 |
A | GLY7 |
A | LYS8 |
A | TRP136 |
A | GLU231 |
A | HOH1190 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE 1PE B 501 |
Chain | Residue |
B | GLY7 |
B | LYS8 |
B | TRP136 |
B | GLU231 |
B | HOH1108 |
B | LYS4 |
site_id | AC3 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE 1PE B 601 |
Chain | Residue |
B | GLN154 |
B | TYR157 |
B | ILE190 |
B | THR195 |
B | TYR206 |
B | PHE215 |
B | HOH1287 |
site_id | AC4 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE 1PE A 701 |
Chain | Residue |
A | GLN154 |
A | TYR157 |
A | PHE189 |
A | ILE190 |
A | THR195 |
A | TYR206 |
A | PHE215 |
A | HOH1188 |
A | HOH1244 |
site_id | AC5 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE MES B 801 |
Chain | Residue |
A | ASP98 |
A | LYS99 |
A | ASP108 |
A | GLN125 |
A | HOH1264 |
B | LEU102 |
B | ARG103 |
B | SER105 |
Functional Information from PROSITE/UniProt
site_id | PS00061 |
Number of Residues | 29 |
Details | ADH_SHORT Short-chain dehydrogenases/reductases family signature. SvvgftgnvgQvnYSTTKAGLiGFTkSLA |
Chain | Residue | Details |
A | SER144-ALA172 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU10001","evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI2 |
Number of Residues | 24 |
Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1ybv |
Chain | Residue | Details |
A | LYS161 | |
A | ASN116 | |
A | SER144 | |
A | TYR157 |
site_id | CSA2 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1ybv |
Chain | Residue | Details |
B | LYS161 | |
B | ASN116 | |
B | SER144 | |
B | TYR157 |
site_id | CSA3 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1ybv |
Chain | Residue | Details |
A | GLN154 | |
A | LYS161 |
site_id | CSA4 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1ybv |
Chain | Residue | Details |
B | GLN154 | |
B | LYS161 |
site_id | CSA5 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1ybv |
Chain | Residue | Details |
A | LYS161 | |
A | TYR157 |
site_id | CSA6 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1ybv |
Chain | Residue | Details |
B | LYS161 | |
B | TYR157 |