3CSL
Structure of the Serratia marcescens hemophore receptor HasR in complex with its hemophore HasA and heme
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005515 | molecular_function | protein binding |
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-dependent 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 | 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-dependent 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 | 12 |
Details | BINDING SITE FOR RESIDUE HEM A 866 |
Chain | Residue |
A | GLY188 |
A | ILE659 |
C | PHE78 |
C | ALA82 |
A | HIS189 |
A | THR357 |
A | THR359 |
A | THR374 |
A | ALA602 |
A | HIS603 |
A | SER606 |
A | GLN608 |
site_id | AC2 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE HEM B 866 |
Chain | Residue |
B | GLY188 |
B | HIS189 |
B | THR357 |
B | THR359 |
B | THR374 |
B | ALA602 |
B | HIS603 |
B | SER606 |
B | GLN608 |
B | ILE659 |
D | PHE78 |
D | ALA82 |
site_id | AC3 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE GOL A 867 |
Chain | Residue |
A | HIS451 |
A | TYR497 |
A | GLY574 |
site_id | AC4 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE GOL A 868 |
Chain | Residue |
A | TRP500 |
A | PRO573 |
site_id | AC5 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE GOL A 871 |
Chain | Residue |
A | TYR584 |
A | TRP622 |
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_FI1 |
Number of Residues | 4 |
Details | BINDING: axial binding residue |
Chain | Residue | Details |
C | HIS32 | |
C | TYR75 | |
D | HIS32 | |
D | TYR75 |