Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004315 | molecular_function | 3-oxoacyl-[acyl-carrier-protein] synthase activity |
A | 0006633 | biological_process | fatty acid biosynthetic process |
A | 0016746 | molecular_function | acyltransferase activity |
A | 0016747 | molecular_function | acyltransferase activity, transferring groups other than amino-acyl groups |
B | 0004315 | molecular_function | 3-oxoacyl-[acyl-carrier-protein] synthase activity |
B | 0006633 | biological_process | fatty acid biosynthetic process |
B | 0016746 | molecular_function | acyltransferase activity |
B | 0016747 | molecular_function | acyltransferase activity, transferring groups other than amino-acyl groups |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE K A 408 |
Chain | Residue |
A | ASN297 |
A | VAL298 |
A | GLU343 |
A | SER388 |
A | ASN389 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE PO4 A 409 |
Chain | Residue |
A | ASP214 |
A | HOH715 |
A | PHE35 |
A | LYS40 |
A | HIS47 |
A | ASN213 |
site_id | AC3 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE EDO A 410 |
Chain | Residue |
A | LYS59 |
A | ILE62 |
A | ASP63 |
site_id | AC4 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE PEG A 411 |
Chain | Residue |
A | ARG45 |
A | GLY206 |
B | LYS128 |
site_id | AC5 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE PEG A 412 |
Chain | Residue |
A | LYS65 |
A | LYS211 |
A | TYR212 |
A | ASP226 |
site_id | AC6 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE PEG A 413 |
Chain | Residue |
A | ALA42 |
A | TRP196 |
A | HOH600 |
B | MSE121 |
site_id | AC7 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE PEG A 414 |
Chain | Residue |
A | THR378 |
A | GLN380 |
site_id | AC8 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE PEG A 415 |
Chain | Residue |
A | ALA287 |
A | GLY288 |
A | VAL289 |
A | ARG315 |
A | HOH594 |
A | HOH597 |
site_id | AC9 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE PEG A 416 |
Chain | Residue |
A | ASP363 |
A | ASN364 |
A | LEU365 |
A | HOH566 |
site_id | BC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE K B 408 |
Chain | Residue |
B | ASN297 |
B | VAL298 |
B | GLU343 |
B | SER388 |
B | ASN389 |
site_id | BC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE PO4 B 409 |
Chain | Residue |
A | HIS253 |
A | LYS407 |
A | HOH657 |
B | HIS253 |
B | HOH595 |
site_id | BC3 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE PO4 B 410 |
Chain | Residue |
B | PHE35 |
B | LYS40 |
B | HIS47 |
B | ASN213 |
B | ASP214 |
B | HOH455 |
B | HOH570 |
site_id | BC4 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE EDO B 412 |
Chain | Residue |
A | GLU28 |
B | ASP63 |
B | PEG414 |
site_id | BC5 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE EDO B 413 |
Chain | Residue |
B | ASP294 |
B | HOH584 |
B | HOH648 |
site_id | BC6 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE PEG B 414 |
Chain | Residue |
B | ASP63 |
B | TYR78 |
B | PRO150 |
B | PHE151 |
B | EDO412 |
B | HOH612 |
site_id | BC7 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE PEG B 415 |
Chain | Residue |
B | LYS65 |
B | LYS211 |
B | ASP226 |
B | ARG227 |
B | ASP228 |
site_id | BC8 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE PGE B 416 |
Chain | Residue |
B | ASP41 |
B | ALA249 |
B | ARG250 |
B | PG4417 |
B | HOH589 |
B | HOH606 |
site_id | BC9 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE PG4 B 417 |
Chain | Residue |
A | ARG122 |
B | ASP41 |
B | GLU245 |
B | LEU248 |
B | PGE416 |
B | HOH509 |
B | HOH510 |
B | HOH515 |
B | HOH657 |
B | HOH663 |
site_id | CC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE PG4 B 418 |
Chain | Residue |
A | LEU127 |
A | LYS128 |
B | ARG45 |
B | ALA204 |
B | GLY206 |
B | THR210 |
Functional Information from PROSITE/UniProt
site_id | PS00606 |
Number of Residues | 17 |
Details | KS3_1 Ketosynthase family 3 (KS3) active site signature. GVNysISsACATSahCI |
Chain | Residue | Details |
A | GLY155-ILE171 | |