4F9J
Structure of Escherichia coli PgaB 42-655 in complex with iron
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
A | 0005515 | molecular_function | protein binding |
A | 0005975 | biological_process | carbohydrate metabolic process |
A | 0009279 | cellular_component | cell outer membrane |
A | 0016020 | cellular_component | membrane |
A | 0016787 | molecular_function | hydrolase activity |
A | 0016810 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds |
A | 0043708 | biological_process | cell adhesion involved in biofilm formation |
A | 0044010 | biological_process | single-species biofilm formation |
A | 0098732 | biological_process | macromolecule deacylation |
B | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
B | 0005515 | molecular_function | protein binding |
B | 0005975 | biological_process | carbohydrate metabolic process |
B | 0009279 | cellular_component | cell outer membrane |
B | 0016020 | cellular_component | membrane |
B | 0016787 | molecular_function | hydrolase activity |
B | 0016810 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds |
B | 0043708 | biological_process | cell adhesion involved in biofilm formation |
B | 0044010 | biological_process | single-species biofilm formation |
B | 0098732 | biological_process | macromolecule deacylation |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE FE A 701 |
Chain | Residue |
A | ASP115 |
A | HIS184 |
A | HIS189 |
A | ACY702 |
A | HOH919 |
site_id | AC2 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE ACY A 702 |
Chain | Residue |
A | HIS189 |
A | PRO251 |
A | TYR252 |
A | LEU274 |
A | FE701 |
A | HIS55 |
A | ASP114 |
A | ASP115 |
A | HIS184 |
site_id | AC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CA A 703 |
Chain | Residue |
A | ASP358 |
A | ASP360 |
A | ASP362 |
A | LEU364 |
A | HOH954 |
A | HOH955 |
site_id | AC4 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE MES A 704 |
Chain | Residue |
A | HIS465 |
A | ASP466 |
A | PHE540 |
A | MSE570 |
A | MSE572 |
A | PRO573 |
A | TYR645 |
A | HOH807 |
A | HOH969 |
A | HOH1129 |
B | ARG215 |
B | HOH948 |
site_id | AC5 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE FE B 701 |
Chain | Residue |
B | ASP115 |
B | HIS184 |
B | HIS189 |
B | ACY702 |
site_id | AC6 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE ACY B 702 |
Chain | Residue |
B | HIS55 |
B | ASP114 |
B | ASP115 |
B | HIS184 |
B | HIS189 |
B | PRO251 |
B | TYR252 |
B | LEU274 |
B | FE701 |
site_id | AC7 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CA B 703 |
Chain | Residue |
B | ASP358 |
B | ASP360 |
B | ASP362 |
B | LEU364 |
B | HOH923 |
B | HOH954 |
site_id | AC8 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE MES B 704 |
Chain | Residue |
A | ARG215 |
A | HOH930 |
A | HOH1017 |
B | HIS465 |
B | ASP466 |
B | PHE540 |
B | MSE570 |
B | MSE572 |
B | PRO573 |
B | TYR645 |
B | HOH808 |
B | HOH968 |
B | HOH1127 |