4F9D
Structure of Escherichia coli PgaB 42-655 in complex with nickel
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 | 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 | 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 NI A 701 |
| Chain | Residue |
| A | ASP115 |
| A | HIS184 |
| A | HIS189 |
| A | ACY702 |
| A | HOH1139 |
| 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 | NI701 |
| 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 | HOH1140 |
| A | HOH1141 |
| site_id | AC4 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE MES A 704 |
| Chain | Residue |
| A | HIS465 |
| A | ASP466 |
| A | PHE540 |
| A | MET570 |
| A | PRO573 |
| A | TYR645 |
| A | HOH807 |
| A | HOH958 |
| A | HOH961 |
| B | ARG215 |
| B | HOH1078 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NI B 701 |
| Chain | Residue |
| B | ASP115 |
| B | HIS184 |
| B | HIS189 |
| B | ACY702 |
| B | HOH1081 |
| 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 | NI701 |
| 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 | HOH1083 |
| B | HOH1085 |
| site_id | AC8 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE MES B 704 |
| Chain | Residue |
| A | ARG215 |
| A | HOH928 |
| B | HIS465 |
| B | ASP466 |
| B | PHE540 |
| B | MET570 |
| B | MET572 |
| B | PRO573 |
| B | TYR645 |
| B | HOH808 |
| B | HOH942 |
| B | HOH1018 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 484 |
| Details | Domain: {"description":"NodB homology","evidences":[{"source":"PROSITE-ProRule","id":"PRU01014","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
