Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003989 | molecular_function | acetyl-CoA carboxylase activity |
A | 0004075 | molecular_function | biotin carboxylase activity |
A | 0005524 | molecular_function | ATP binding |
A | 0006633 | biological_process | fatty acid biosynthetic process |
A | 0016874 | molecular_function | ligase activity |
A | 0046872 | molecular_function | metal ion binding |
A | 2001295 | biological_process | malonyl-CoA biosynthetic process |
B | 0003989 | molecular_function | acetyl-CoA carboxylase activity |
B | 0004075 | molecular_function | biotin carboxylase activity |
B | 0005524 | molecular_function | ATP binding |
B | 0006633 | biological_process | fatty acid biosynthetic process |
B | 0016874 | molecular_function | ligase activity |
B | 0046872 | molecular_function | metal ion binding |
B | 2001295 | biological_process | malonyl-CoA biosynthetic process |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE GOL A 452 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GOL A 457 |
Chain | Residue |
A | TRP183 |
A | SER184 |
A | HOH572 |
A | HOH612 |
B | PHE347 |
B | PRO349 |
site_id | AC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CA A 458 |
Chain | Residue |
A | ASN291 |
A | ANP460 |
A | HOH588 |
A | GLU289 |
site_id | AC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CA A 459 |
Chain | Residue |
A | GLU276 |
A | GLU289 |
A | ANP460 |
A | HOH478 |
site_id | AC5 |
Number of Residues | 24 |
Details | BINDING SITE FOR RESIDUE ANP A 460 |
Chain | Residue |
A | LYS117 |
A | ILE132 |
A | ILE157 |
A | LYS159 |
A | GLY164 |
A | GLY165 |
A | GLY166 |
A | MSE169 |
A | GLU201 |
A | LYS202 |
A | TYR203 |
A | ILE204 |
A | HIS209 |
A | GLN233 |
A | HIS236 |
A | GLU276 |
A | LEU278 |
A | GLU289 |
A | THR437 |
A | CA458 |
A | CA459 |
A | HOH531 |
A | HOH603 |
A | HOH715 |
site_id | AC6 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE CAC A 461 |
Chain | Residue |
A | MSE114 |
A | SER115 |
A | LYS117 |
A | ALA161 |
A | ALA162 |
A | GLY163 |
A | HOH533 |
A | HOH561 |
A | HOH588 |
A | HOH730 |
A | HOH732 |
site_id | AC7 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE GOL B 453 |
Chain | Residue |
A | ASP39 |
A | TYR372 |
A | HOH648 |
B | LYS356 |
B | ILE358 |
site_id | AC8 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE GOL B 454 |
Chain | Residue |
B | LYS38 |
B | HOH570 |
site_id | AC9 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CA B 455 |
Chain | Residue |
B | GLU276 |
B | GLU289 |
B | ANP457 |
B | HOH610 |
site_id | BC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CA B 456 |
Chain | Residue |
B | GLU289 |
B | ASN291 |
B | ANP457 |
B | HOH611 |
B | HOH684 |
site_id | BC2 |
Number of Residues | 30 |
Details | BINDING SITE FOR RESIDUE ANP B 457 |
Chain | Residue |
B | LYS117 |
B | ILE132 |
B | ILE157 |
B | LYS159 |
B | GLY164 |
B | GLY165 |
B | GLY166 |
B | MSE169 |
B | GLU201 |
B | LYS202 |
B | TYR203 |
B | ILE204 |
B | HIS209 |
B | GLN233 |
B | HIS236 |
B | GLU276 |
B | LEU278 |
B | GLU289 |
B | THR437 |
B | HOH444 |
B | CA455 |
B | CA456 |
B | HOH508 |
B | HOH583 |
B | HOH584 |
B | HOH585 |
B | HOH610 |
B | HOH615 |
B | HOH717 |
B | HOH736 |
site_id | BC3 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE CAC B 458 |
Chain | Residue |
B | LYS117 |
B | ALA161 |
B | ALA162 |
B | GLY163 |
B | HOH560 |
B | HOH612 |
B | HOH684 |
B | MSE114 |
B | SER115 |
site_id | BC4 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE FMT B 459 |
Chain | Residue |
B | SER344 |
B | LYS415 |
B | THR416 |
Functional Information from PROSITE/UniProt
site_id | PS00866 |
Number of Residues | 15 |
Details | CPSASE_1 Carbamoyl-phosphate synthase subdomain signature 1. YPVILKAAaggGGrG |
Chain | Residue | Details |
A | TYR154-GLY168 | |
site_id | PS00867 |
Number of Residues | 8 |
Details | CPSASE_2 Carbamoyl-phosphate synthase subdomain signature 2. FIEMNTRL |
Chain | Residue | Details |
A | PHE287-LEU294 | |