2FAD
Crystal structure of E. coli heptanoyl-ACP
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000035 | molecular_function | acyl binding |
| A | 0000036 | molecular_function | acyl carrier activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0006633 | biological_process | fatty acid biosynthetic process |
| A | 0008289 | molecular_function | lipid binding |
| A | 0008610 | biological_process | lipid biosynthetic process |
| A | 0009245 | biological_process | lipid A biosynthetic process |
| A | 0009410 | biological_process | response to xenobiotic stimulus |
| A | 0031177 | molecular_function | phosphopantetheine binding |
| B | 0000035 | molecular_function | acyl binding |
| B | 0000036 | molecular_function | acyl carrier activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0006633 | biological_process | fatty acid biosynthetic process |
| B | 0008289 | molecular_function | lipid binding |
| B | 0008610 | biological_process | lipid biosynthetic process |
| B | 0009245 | biological_process | lipid A biosynthetic process |
| B | 0009410 | biological_process | response to xenobiotic stimulus |
| B | 0031177 | molecular_function | phosphopantetheine binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE NA A 401 |
| Chain | Residue |
| A | SER1 |
| B | ASP51 |
| B | ALA77 |
| B | HOH472 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 402 |
| Chain | Residue |
| A | GLU5 |
| A | GLU53 |
| B | GLU48 |
| B | HOH411 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN A 403 |
| Chain | Residue |
| A | HOH459 |
| A | HOH507 |
| B | ASP35 |
| B | ASP38 |
| A | GLU21 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 404 |
| Chain | Residue |
| A | ASP35 |
| A | HOH464 |
| A | HOH513 |
| B | GLU21 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ZN A 405 |
| Chain | Residue |
| A | ASP56 |
| A | HOH427 |
| A | HOH428 |
| A | HOH478 |
| A | HOH479 |
| A | HOH480 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 406 |
| Chain | Residue |
| A | GLU48 |
| B | GLU5 |
| B | GLU53 |
| B | HOH428 |
| site_id | AC7 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE ZN A 407 |
| Chain | Residue |
| A | ALA77 |
| A | ALA77 |
| A | HOH433 |
| A | HOH433 |
| A | HOH434 |
| A | HOH434 |
| A | HOH496 |
| A | HOH496 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 408 |
| Chain | Residue |
| A | ASN25 |
| A | GLU57 |
| A | GLU60 |
| B | GLU30 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN B 409 |
| Chain | Residue |
| B | ASP56 |
| B | HOH446 |
| B | HOH464 |
| B | HOH476 |
| site_id | BC1 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE PM5 A 301 |
| Chain | Residue |
| A | PHE28 |
| A | SER36 |
| A | THR39 |
| A | VAL43 |
| A | LEU46 |
| A | THR52 |
| A | ALA59 |
| A | GLU60 |
| A | ILE62 |
| A | HOH520 |
| site_id | BC2 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE PM5 B 302 |
| Chain | Residue |
| A | HOH526 |
| B | PHE28 |
| B | VAL29 |
| B | SER36 |
| B | LEU46 |
| B | ILE54 |
| B | ALA59 |
| B | GLU60 |
| B | ILE62 |
| B | HOH453 |
| B | HOH470 |
Functional Information from PROSITE/UniProt
| site_id | PS00012 |
| Number of Residues | 16 |
| Details | PHOSPHOPANTETHEINE Phosphopantetheine attachment site. DLGADSLDTVELVMAL |
| Chain | Residue | Details |
| A | ASP31-LEU46 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | MOD_RES: O-(pantetheine 4'-phosphoryl)serine => ECO:0000255|PROSITE-ProRule:PRU00258, ECO:0000269|PubMed:4882207 |
| Chain | Residue | Details |
| A | LEU37 | |
| B | LEU37 |
