3DDR
Structure of the Serratia marcescens hemophore receptor HasR-Ile671Gly mutant in complex with its hemophore HasA and heme
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005515 | molecular_function | protein binding |
| A | 0006826 | biological_process | iron ion transport |
| A | 0009279 | cellular_component | cell outer membrane |
| A | 0015232 | molecular_function | heme transmembrane transporter activity |
| A | 0015344 | molecular_function | siderophore uptake transmembrane transporter activity |
| A | 0015886 | biological_process | heme transport |
| A | 0019867 | cellular_component | outer membrane |
| A | 0022857 | molecular_function | transmembrane transporter activity |
| A | 0033214 | biological_process | siderophore-iron import into cell |
| A | 0044718 | biological_process | siderophore transmembrane transport |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0055085 | biological_process | transmembrane transport |
| B | 0005515 | molecular_function | protein binding |
| B | 0006826 | biological_process | iron ion transport |
| B | 0009279 | cellular_component | cell outer membrane |
| B | 0015232 | molecular_function | heme transmembrane transporter activity |
| B | 0015344 | molecular_function | siderophore uptake transmembrane transporter activity |
| B | 0015886 | biological_process | heme transport |
| B | 0019867 | cellular_component | outer membrane |
| B | 0022857 | molecular_function | transmembrane transporter activity |
| B | 0033214 | biological_process | siderophore-iron import into cell |
| B | 0044718 | biological_process | siderophore transmembrane transport |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0055085 | biological_process | transmembrane transport |
| C | 0005515 | molecular_function | protein binding |
| C | 0005576 | cellular_component | extracellular region |
| C | 0046872 | molecular_function | metal ion binding |
| D | 0005515 | molecular_function | protein binding |
| D | 0005576 | cellular_component | extracellular region |
| D | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE NA A 866 |
| Chain | Residue |
| A | HIS189 |
| A | HIS603 |
| site_id | AC2 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE NA B 866 |
| Chain | Residue |
| B | HIS189 |
| B | HIS603 |
| site_id | AC3 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE HEM C 200 |
| Chain | Residue |
| C | TYR75 |
| C | HIS83 |
| C | HIS133 |
| C | TYR137 |
| C | MET140 |
| A | HIS603 |
| A | SER605 |
| A | GLY671 |
| A | GLY672 |
| C | TYR55 |
| site_id | AC4 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE HEM D 200 |
| Chain | Residue |
| B | HIS603 |
| B | SER605 |
| B | GLY671 |
| B | GLY672 |
| D | TYR55 |
| D | TYR75 |
| D | HIS83 |
| D | LEU85 |
| D | HIS133 |
| D | TYR137 |
| site_id | AC5 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE GOL B 867 |
| Chain | Residue |
| B | ARG327 |
| B | LEU328 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL A 867 |
| Chain | Residue |
| A | SER234 |
| A | ASP235 |
| A | LEU237 |
| A | LYS241 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE GOL B 869 |
| Chain | Residue |
| B | ASP118 |
| B | ARG454 |
| B | ASP496 |
| site_id | AC8 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE GOL B 871 |
| Chain | Residue |
| B | HIS321 |
| B | ARG373 |
| B | TYR376 |
Functional Information from PROSITE/UniProt
| site_id | PS00430 |
| Number of Residues | 107 |
| Details | TONB_DEPENDENT_REC_1 TonB-dependent receptor (TBDR) proteins signature 1. aqaeassaqaaqqknfniaaqplqsamlrfaeqagmqvffdevkldgmqaaalngsmsveqglrrliggnpvafrlqpqgqivlsrlptangdggalal................DSLTVLGA |
| Chain | Residue | Details |
| A | ALA1-ALA107 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Binding site: {"description":"axial binding residue"} |
| Chain | Residue | Details |
