5FBT
Crystal structure of rifampin phosphotransferase RPH-Lm from Listeria monocytogenes in complex with rifampin
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003824 | molecular_function | catalytic activity |
A | 0005524 | molecular_function | ATP binding |
A | 0016301 | molecular_function | kinase activity |
A | 0016310 | biological_process | phosphorylation |
A | 0016772 | molecular_function | transferase activity, transferring phosphorus-containing groups |
A | 0046677 | biological_process | response to antibiotic |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 11 |
Details | binding site for residue 5WQ A 901 |
Chain | Residue |
A | VAL333 |
A | HOH1004 |
A | HOH1040 |
A | TYR351 |
A | THR355 |
A | PRO356 |
A | ALA357 |
A | VAL368 |
A | MSE383 |
A | LEU387 |
A | PHE479 |
site_id | AC2 |
Number of Residues | 4 |
Details | binding site for residue CL A 902 |
Chain | Residue |
A | LYS551 |
A | LYS551 |
A | ASN552 |
A | ASN552 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | ACT_SITE: Tele-phosphohistidine intermediate => ECO:0000269|PubMed:27103605, ECO:0000305|PubMed:27001859 |
Chain | Residue | Details |
A | HIS825 |
site_id | SWS_FT_FI2 |
Number of Residues | 3 |
Details | BINDING: BINDING => ECO:0000305|PubMed:27001859, ECO:0000305|PubMed:27103605, ECO:0000312|PDB:5HV1, ECO:0007744|PDB:5FBS |
Chain | Residue | Details |
A | LYS22 | |
A | ARG117 | |
A | THR136 |
site_id | SWS_FT_FI3 |
Number of Residues | 5 |
Details | BINDING: BINDING => ECO:0000305|PubMed:27001859, ECO:0000312|PDB:5HV1 |
Chain | Residue | Details |
A | GLY132 | |
A | GLN183 | |
A | GLU297 | |
A | GLN309 | |
A | ARG311 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000269|PubMed:27103605 |
Chain | Residue | Details |
A | GLN336 | |
A | TYR351 |