2FHS
Structure of Acyl Carrier Protein Bound to FabI, the Enoyl Reductase from Escherichia Coli
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004318 | molecular_function | enoyl-[acyl-carrier-protein] reductase (NADH) activity |
A | 0005515 | molecular_function | protein binding |
A | 0005829 | cellular_component | cytosol |
A | 0006629 | biological_process | lipid metabolic process |
A | 0006631 | biological_process | fatty acid metabolic process |
A | 0006633 | biological_process | fatty acid biosynthetic process |
A | 0008610 | biological_process | lipid biosynthetic process |
A | 0009102 | biological_process | biotin biosynthetic process |
A | 0016020 | cellular_component | membrane |
A | 0016491 | molecular_function | oxidoreductase activity |
A | 0030497 | biological_process | fatty acid elongation |
A | 0032991 | cellular_component | protein-containing complex |
A | 0042802 | molecular_function | identical protein binding |
A | 0046677 | biological_process | response to antibiotic |
A | 0051289 | biological_process | protein homotetramerization |
A | 0070404 | molecular_function | NADH binding |
A | 1902494 | cellular_component | catalytic complex |
B | 0004318 | molecular_function | enoyl-[acyl-carrier-protein] reductase (NADH) activity |
B | 0005515 | molecular_function | protein binding |
B | 0005829 | cellular_component | cytosol |
B | 0006629 | biological_process | lipid metabolic process |
B | 0006631 | biological_process | fatty acid metabolic process |
B | 0006633 | biological_process | fatty acid biosynthetic process |
B | 0008610 | biological_process | lipid biosynthetic process |
B | 0009102 | biological_process | biotin biosynthetic process |
B | 0016020 | cellular_component | membrane |
B | 0016491 | molecular_function | oxidoreductase activity |
B | 0030497 | biological_process | fatty acid elongation |
B | 0032991 | cellular_component | protein-containing complex |
B | 0042802 | molecular_function | identical protein binding |
B | 0046677 | biological_process | response to antibiotic |
B | 0051289 | biological_process | protein homotetramerization |
B | 0070404 | molecular_function | NADH binding |
B | 1902494 | cellular_component | catalytic complex |
C | 0000035 | molecular_function | acyl binding |
C | 0000036 | molecular_function | acyl carrier activity |
C | 0005515 | molecular_function | protein binding |
C | 0005737 | cellular_component | cytoplasm |
C | 0005829 | cellular_component | cytosol |
C | 0006629 | biological_process | lipid metabolic process |
C | 0006631 | biological_process | fatty acid metabolic process |
C | 0006633 | biological_process | fatty acid biosynthetic process |
C | 0008289 | molecular_function | lipid binding |
C | 0008610 | biological_process | lipid biosynthetic process |
C | 0009245 | biological_process | lipid A biosynthetic process |
C | 0009410 | biological_process | response to xenobiotic stimulus |
C | 0016020 | cellular_component | membrane |
C | 0031177 | molecular_function | phosphopantetheine binding |
Functional Information from PROSITE/UniProt
site_id | PS00012 |
Number of Residues | 16 |
Details | PHOSPHOPANTETHEINE Phosphopantetheine attachment site. DLGADSLDTVELVMAL |
Chain | Residue | Details |
C | ASP32-LEU47 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 4 |
Details | ACT_SITE: Proton acceptor => ECO:0000250 |
Chain | Residue | Details |
A | TYR146 | |
A | TYR156 | |
B | TYR146 | |
B | TYR156 |
site_id | SWS_FT_FI2 |
Number of Residues | 14 |
Details | BINDING: BINDING => ECO:0000269|PubMed:10201369, ECO:0000269|PubMed:10398587, ECO:0000269|PubMed:10493822, ECO:0000269|PubMed:10595560, ECO:0000269|PubMed:11514139, ECO:0000269|PubMed:12109908, ECO:0000269|PubMed:12699381, ECO:0000269|PubMed:8953047 |
Chain | Residue | Details |
A | GLY13 | |
B | GLN40 | |
B | ASP64 | |
B | ILE92 | |
B | LYS163 | |
B | ILE192 | |
A | SER19 | |
A | GLN40 | |
A | ASP64 | |
A | ILE92 | |
A | LYS163 | |
A | ILE192 | |
B | GLY13 | |
B | SER19 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | BINDING: |
Chain | Residue | Details |
A | ALA95 | |
B | ALA95 |
site_id | SWS_FT_FI4 |
Number of Residues | 6 |
Details | SITE: Involved in acyl-ACP binding |
Chain | Residue | Details |
A | LYS201 | |
A | ARG204 | |
A | LYS205 | |
B | LYS201 | |
B | ARG204 | |
B | LYS205 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1qsg |
Chain | Residue | Details |
A | GLU150 |
site_id | CSA2 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1qsg |
Chain | Residue | Details |
B | GLU150 |
site_id | CSA3 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1qsg |
Chain | Residue | Details |
A | TYR156 | |
A | LYS163 |
site_id | CSA4 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1qsg |
Chain | Residue | Details |
B | TYR156 | |
B | LYS163 |
site_id | CSA5 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1qsg |
Chain | Residue | Details |
A | MET159 | |
A | LYS163 |
site_id | CSA6 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1qsg |
Chain | Residue | Details |
B | MET159 | |
B | LYS163 |
site_id | MCSA1 |
Number of Residues | 2 |
Details | M-CSA 606 |
Chain | Residue | Details |
A | TYR156 | proton acceptor, proton donor |
A | LYS163 | electrostatic stabiliser |
site_id | MCSA2 |
Number of Residues | 2 |
Details | M-CSA 606 |
Chain | Residue | Details |
B | TYR156 | proton acceptor, proton donor |
B | LYS163 | electrostatic stabiliser |