2FAC
Crystal structure of E. coli hexanoyl-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 | 0006629 | biological_process | lipid metabolic process |
A | 0006631 | biological_process | fatty acid metabolic process |
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 | 0006629 | biological_process | lipid metabolic process |
B | 0006631 | biological_process | fatty acid metabolic process |
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 ZN A 401 |
Chain | Residue |
A | SER1 |
A | HOH515 |
B | ASP51 |
B | ALA77 |
site_id | AC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN A 402 |
Chain | Residue |
A | GLU21 |
A | HOH421 |
B | ASP35 |
B | ASP38 |
site_id | AC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ZN A 403 |
Chain | Residue |
A | HOH424 |
A | HOH426 |
A | HOH479 |
A | HOH498 |
A | ASP31 |
site_id | AC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN A 404 |
Chain | Residue |
A | ASP35 |
A | HOH448 |
A | HOH468 |
B | GLU21 |
site_id | AC5 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE ZN A 405 |
Chain | Residue |
A | ASP56 |
A | HOH412 |
A | HOH433 |
A | HOH434 |
A | HOH473 |
A | HOH492 |
site_id | AC6 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN A 406 |
Chain | Residue |
A | GLU5 |
A | GLU53 |
B | GLU48 |
B | HOH415 |
site_id | AC7 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN B 407 |
Chain | Residue |
A | GLU48 |
A | HOH453 |
B | GLU5 |
B | GLU53 |
site_id | AC8 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE ZN A 408 |
Chain | Residue |
A | ALA77 |
A | ALA77 |
A | HOH458 |
A | HOH458 |
A | HOH459 |
A | HOH459 |
A | HOH460 |
A | HOH460 |
site_id | AC9 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ZN B 409 |
Chain | Residue |
B | ASP56 |
B | HOH449 |
B | HOH450 |
B | HOH475 |
B | HOH482 |
site_id | BC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ZN B 410 |
Chain | Residue |
B | ASP51 |
B | HOH431 |
B | HOH432 |
B | HOH439 |
B | HOH488 |
site_id | BC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ZN B 411 |
Chain | Residue |
A | ASN25 |
A | GLU57 |
A | GLU60 |
A | HOH436 |
B | GLU30 |
site_id | BC3 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE PM4 A 301 |
Chain | Residue |
A | PHE28 |
A | ASP35 |
A | SER36 |
A | THR39 |
A | VAL43 |
A | ILE54 |
A | ALA59 |
A | GLU60 |
A | ILE62 |
A | HOH423 |
A | HOH483 |
A | HOH520 |
site_id | BC4 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE PM4 B 302 |
Chain | Residue |
B | PHE28 |
B | SER36 |
B | THR39 |
B | VAL43 |
B | LEU46 |
B | GLU47 |
B | THR52 |
B | ILE54 |
B | ALA59 |
B | ILE62 |
B | ILE72 |
B | HOH500 |
B | HOH507 |
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 |