Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000035 | molecular_function | acyl binding |
| A | 0000036 | molecular_function | acyl carrier activity |
| A | 0005737 | cellular_component | cytoplasm |
| 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 | 0009245 | biological_process | lipid A biosynthetic process |
| A | 0016020 | cellular_component | membrane |
| B | 0000035 | molecular_function | acyl binding |
| B | 0000036 | molecular_function | acyl carrier activity |
| B | 0005737 | cellular_component | cytoplasm |
| 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 | 0009245 | biological_process | lipid A biosynthetic process |
| B | 0016020 | cellular_component | membrane |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | binding site for residue ZN A 101 |
| Chain | Residue |
| A | GLU53 |
| A | HOH208 |
| A | HOH209 |
| B | GLU5 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | binding site for residue ZN A 102 |
| Chain | Residue |
| A | GLU17 |
| A | ASP71 |
| A | HOH209 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | binding site for residue ZN A 103 |
| Chain | Residue |
| A | HOH202 |
| A | ASP45 |
| A | ASP49 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | binding site for residue ZN A 104 |
| Chain | Residue |
| A | GLU23 |
| A | HOH204 |
| A | HOH207 |
| B | HOH203 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | binding site for residue ZN B 101 |
| Chain | Residue |
| A | GLU5 |
| B | GLU53 |
| B | HOH208 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | binding site for residue ZN B 102 |
| Chain | Residue |
| B | GLU17 |
| B | ASP71 |
| B | HOH204 |
| B | HOH208 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | binding site for residue ZN B 103 |
| Chain | Residue |
| B | ASP45 |
| B | ASP49 |
| B | HOH202 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | binding site for residue ZN B 104 |
| Chain | Residue |
| A | ASP39 |
| A | ASP42 |
| A | HOH201 |
| B | ASP39 |
| B | ASP42 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | binding site for residue ZN B 105 |
| Chain | Residue |
| A | SER3 |
| A | HOH203 |
| A | HOH206 |
| B | LYS12 |
| B | GLU23 |
| B | HOH201 |
Functional Information from PROSITE/UniProt
| site_id | PS00012 |
| Number of Residues | 16 |
| Details | PHOSPHOPANTETHEINE Phosphopantetheine attachment site. DLGADSLDLVDLVMDF |
| Chain | Residue | Details |
| A | ASP35-PHE50 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 150 |
| Details | Domain: {"description":"Carrier","evidences":[{"source":"PROSITE-ProRule","id":"PRU00258","evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"O-(pantetheine 4'-phosphoryl)serine","evidences":[{"source":"PROSITE-ProRule","id":"PRU00258","evidenceCode":"ECO:0000255"}]} |
