Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003824 | molecular_function | catalytic activity |
A | 0005737 | cellular_component | cytoplasm |
A | 0008360 | biological_process | regulation of cell shape |
A | 0008760 | molecular_function | UDP-N-acetylglucosamine 1-carboxyvinyltransferase activity |
A | 0009252 | biological_process | peptidoglycan biosynthetic process |
A | 0016740 | molecular_function | transferase activity |
A | 0016765 | molecular_function | transferase activity, transferring alkyl or aryl (other than methyl) groups |
A | 0019277 | biological_process | UDP-N-acetylgalactosamine biosynthetic process |
A | 0051301 | biological_process | cell division |
A | 0071555 | biological_process | cell wall organization |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE PG4 A 501 |
Chain | Residue |
A | ASP132 |
A | LYS139 |
A | VAL145 |
A | ASN350 |
A | HOH898 |
A | HOH928 |
site_id | AC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE PG4 A 502 |
Chain | Residue |
A | GLU361 |
A | LYS326 |
A | THR352 |
A | TYR359 |
site_id | AC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE PG4 A 503 |
Chain | Residue |
A | GLU255 |
A | LEU257 |
A | ARG267 |
A | ARG288 |
A | HOH703 |
A | HOH935 |
site_id | AC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE PGE A 504 |
Chain | Residue |
A | LYS165 |
A | PHE166 |
A | ASP167 |
A | ASN192 |
site_id | AC5 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE PEG A 505 |
Chain | Residue |
A | PRO47 |
A | THR49 |
A | PHE231 |
A | THR232 |
A | HOH901 |
site_id | AC6 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE PEG A 506 |
Chain | Residue |
A | ALA323 |
A | LYS324 |
A | VAL363 |
A | GLU364 |
A | HOH845 |
site_id | AC7 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE EDO A 507 |
Chain | Residue |
A | ILE90 |
A | TYR151 |
A | TYR153 |
site_id | AC8 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE EDO A 508 |
site_id | AC9 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE EDO A 509 |
Chain | Residue |
A | ARG112 |
A | GLY114 |
site_id | BC1 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE EDO A 510 |
Chain | Residue |
A | GLU146 |
A | ARG148 |
A | TYR153 |
site_id | BC2 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE EDO A 511 |
site_id | BC3 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE EDO A 512 |
site_id | BC4 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE EDO A 513 |
Chain | Residue |
A | ASN284 |
A | GLY285 |
A | ASN286 |
site_id | BC5 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE EDO A 514 |
Chain | Residue |
A | LYS214 |
A | TYR221 |
A | ARG365 |
site_id | BC6 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE EDO A 515 |
Chain | Residue |
A | HIS163 |
A | GLU191 |
site_id | BC7 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE EDO A 516 |
Chain | Residue |
A | GLU187 |
A | LYS223 |
A | GLN390 |
site_id | BC8 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE EDO A 517 |
Chain | Residue |
A | LEU43 |
A | GLU45 |
A | GLU226 |
A | HOH701 |
A | HOH863 |
site_id | BC9 |
Number of Residues | 32 |
Details | BINDING SITE FOR RESIDUE EPZ A 518 |
Chain | Residue |
A | LYS31 |
A | ASN32 |
A | ALA101 |
A | ARG129 |
A | PRO130 |
A | ILE131 |
A | ASP132 |
A | GLN133 |
A | LEU168 |
A | THR170 |
A | VAL171 |
A | THR172 |
A | THR310 |
A | ASP311 |
A | ILE333 |
A | PHE334 |
A | VAL353 |
A | LEU376 |
A | HOH604 |
A | HOH609 |
A | HOH615 |
A | HOH624 |
A | HOH628 |
A | HOH633 |
A | HOH635 |
A | HOH638 |
A | HOH640 |
A | HOH641 |
A | HOH648 |
A | HOH804 |
A | HOH805 |
A | HOH807 |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
A | QPA124 | |
Chain | Residue | Details |
A | LYS31 | |
Chain | Residue | Details |
A | ARG100 | |
Chain | Residue | Details |
A | ARG129 | |
A | THR170 | |
A | ASP311 | |
A | ILE333 | |
Chain | Residue | Details |
A | QPA124 | |