1XPR
Structural mechanism of inhibition of the Rho transcription termination factor by the antibiotic 5a-formylbicyclomycin (FB)
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0003676 | molecular_function | nucleic acid binding |
| A | 0003723 | molecular_function | RNA binding |
| A | 0004386 | molecular_function | helicase activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005829 | cellular_component | cytosol |
| A | 0006353 | biological_process | DNA-templated transcription termination |
| A | 0008186 | molecular_function | ATP-dependent activity, acting on RNA |
| A | 0016020 | cellular_component | membrane |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0042802 | molecular_function | identical protein binding |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0003676 | molecular_function | nucleic acid binding |
| B | 0003723 | molecular_function | RNA binding |
| B | 0004386 | molecular_function | helicase activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0005524 | molecular_function | ATP binding |
| B | 0005829 | cellular_component | cytosol |
| B | 0006353 | biological_process | DNA-templated transcription termination |
| B | 0008186 | molecular_function | ATP-dependent activity, acting on RNA |
| B | 0016020 | cellular_component | membrane |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0042802 | molecular_function | identical protein binding |
| C | 0000166 | molecular_function | nucleotide binding |
| C | 0003676 | molecular_function | nucleic acid binding |
| C | 0003723 | molecular_function | RNA binding |
| C | 0004386 | molecular_function | helicase activity |
| C | 0005515 | molecular_function | protein binding |
| C | 0005524 | molecular_function | ATP binding |
| C | 0005829 | cellular_component | cytosol |
| C | 0006353 | biological_process | DNA-templated transcription termination |
| C | 0008186 | molecular_function | ATP-dependent activity, acting on RNA |
| C | 0016020 | cellular_component | membrane |
| C | 0016787 | molecular_function | hydrolase activity |
| C | 0042802 | molecular_function | identical protein binding |
| D | 0000166 | molecular_function | nucleotide binding |
| D | 0003676 | molecular_function | nucleic acid binding |
| D | 0003723 | molecular_function | RNA binding |
| D | 0004386 | molecular_function | helicase activity |
| D | 0005515 | molecular_function | protein binding |
| D | 0005524 | molecular_function | ATP binding |
| D | 0005829 | cellular_component | cytosol |
| D | 0006353 | biological_process | DNA-templated transcription termination |
| D | 0008186 | molecular_function | ATP-dependent activity, acting on RNA |
| D | 0016020 | cellular_component | membrane |
| D | 0016787 | molecular_function | hydrolase activity |
| D | 0042802 | molecular_function | identical protein binding |
| E | 0000166 | molecular_function | nucleotide binding |
| E | 0003676 | molecular_function | nucleic acid binding |
| E | 0003723 | molecular_function | RNA binding |
| E | 0004386 | molecular_function | helicase activity |
| E | 0005515 | molecular_function | protein binding |
| E | 0005524 | molecular_function | ATP binding |
| E | 0005829 | cellular_component | cytosol |
| E | 0006353 | biological_process | DNA-templated transcription termination |
| E | 0008186 | molecular_function | ATP-dependent activity, acting on RNA |
| E | 0016020 | cellular_component | membrane |
| E | 0016787 | molecular_function | hydrolase activity |
| E | 0042802 | molecular_function | identical protein binding |
| F | 0000166 | molecular_function | nucleotide binding |
| F | 0003676 | molecular_function | nucleic acid binding |
| F | 0003723 | molecular_function | RNA binding |
| F | 0004386 | molecular_function | helicase activity |
| F | 0005515 | molecular_function | protein binding |
| F | 0005524 | molecular_function | ATP binding |
| F | 0005829 | cellular_component | cytosol |
| F | 0006353 | biological_process | DNA-templated transcription termination |
| F | 0008186 | molecular_function | ATP-dependent activity, acting on RNA |
| F | 0016020 | cellular_component | membrane |
| F | 0016787 | molecular_function | hydrolase activity |
| F | 0042802 | molecular_function | identical protein binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MG A 1601 |
| Chain | Residue |
| A | THR185 |
| A | GLU215 |
| A | AGS1600 |
| site_id | AC2 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE MG B 2601 |
| Chain | Residue |
| B | THR185 |
| B | AGS2600 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG C 3601 |
| Chain | Residue |
| C | LYS184 |
| C | THR185 |
| C | AGS3600 |
| C | FB3701 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MG D 4601 |
| Chain | Residue |
| D | THR185 |
| D | AGS4600 |
| D | FB4701 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG E 5601 |
| Chain | Residue |
| E | THR185 |
| E | GLU211 |
| E | ARG212 |
| E | AGS5600 |
| E | FB5701 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG F 6601 |
| Chain | Residue |
| F | THR185 |
| F | ARG212 |
| F | GLU215 |
| F | AGS6600 |
| F | FB6701 |
| site_id | AC7 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE AGS A 1600 |
| Chain | Residue |
| A | THR158 |
| A | LYS181 |
| A | ALA182 |
| A | GLY183 |
| A | LYS184 |
| A | THR185 |
| A | MET186 |
| A | PHE355 |
| A | MG1601 |
| site_id | AC8 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE AGS B 2600 |
| Chain | Residue |
| A | ARG366 |
| A | LYS367 |
| B | PRO180 |
| B | LYS181 |
| B | ALA182 |
| B | GLY183 |
| B | LYS184 |
| B | THR185 |
| B | MET186 |
| B | ARG212 |
| B | PHE355 |
| B | PRO356 |
| B | MG2601 |
| B | FB2701 |
| site_id | AC9 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE AGS C 3600 |
| Chain | Residue |
| B | ARG366 |
| C | THR158 |
| C | PRO180 |
| C | LYS181 |
| C | ALA182 |
| C | GLY183 |
| C | LYS184 |
| C | THR185 |
| C | MET186 |
| C | MG3601 |
| C | FB3701 |
| site_id | BC1 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE AGS D 4600 |
| Chain | Residue |
| C | ARG366 |
| C | LYS367 |
| D | PRO180 |
| D | LYS181 |
| D | ALA182 |
| D | GLY183 |
| D | LYS184 |
| D | THR185 |
| D | MET186 |
| D | ARG212 |
| D | PHE355 |
| D | MG4601 |
| D | FB4701 |
| site_id | BC2 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE AGS E 5600 |
| Chain | Residue |
| D | ARG366 |
| E | THR158 |
| E | PRO180 |
| E | LYS181 |
| E | ALA182 |
| E | GLY183 |
| E | LYS184 |
| E | THR185 |
| E | MET186 |
| E | ARG212 |
| E | PHE355 |
| E | MG5601 |
| E | FB5701 |
| site_id | BC3 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE AGS F 6600 |
| Chain | Residue |
| E | ARG366 |
| E | GLU369 |
| F | THR158 |
| F | PRO180 |
| F | LYS181 |
| F | ALA182 |
| F | GLY183 |
| F | LYS184 |
| F | THR185 |
| F | MET186 |
| F | ARG212 |
| F | PHE355 |
| F | MG6601 |
| F | FB6701 |
| site_id | BC4 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE FB B 2701 |
| Chain | Residue |
| B | LYS184 |
| B | ASP210 |
| B | GLU211 |
| B | ARG212 |
| B | ASP265 |
| B | SER266 |
| B | LEU320 |
| B | THR323 |
| B | AGS2600 |
| A | LYS336 |
| A | GLY337 |
| B | PRO180 |
| site_id | BC5 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE FB C 3701 |
| Chain | Residue |
| B | LYS336 |
| B | GLY337 |
| C | LYS184 |
| C | ILE209 |
| C | ASP210 |
| C | GLU211 |
| C | ASP265 |
| C | SER266 |
| C | ARG269 |
| C | THR323 |
| C | AGS3600 |
| C | MG3601 |
| site_id | BC6 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE FB D 4701 |
| Chain | Residue |
| C | LYS336 |
| C | GLY337 |
| D | ASP210 |
| D | GLU211 |
| D | ASP265 |
| D | SER266 |
| D | ARG269 |
| D | LEU320 |
| D | THR323 |
| D | AGS4600 |
| D | MG4601 |
| site_id | BC7 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE FB E 5701 |
| Chain | Residue |
| D | LYS336 |
| D | GLY337 |
| E | LYS184 |
| E | ILE209 |
| E | ASP210 |
| E | GLU211 |
| E | ARG212 |
| E | ASP265 |
| E | SER266 |
| E | ARG269 |
| E | LEU320 |
| E | THR323 |
| E | AGS5600 |
| E | MG5601 |
| site_id | BC8 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE FB F 6701 |
| Chain | Residue |
| E | LYS336 |
| E | GLY337 |
| E | ARG366 |
| F | LYS184 |
| F | ILE209 |
| F | ASP210 |
| F | GLU211 |
| F | ARG212 |
| F | ASP265 |
| F | SER266 |
| F | ARG269 |
| F | THR323 |
| F | AGS6600 |
| F | MG6601 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 450 |
| Details | Domain: {"description":"Rho RNA-BD","evidences":[{"source":"PROSITE-ProRule","id":"PRU01203","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 54 |
| Details | Region: {"description":"RNA-binding 1"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 20 |
| Details | Region: {"description":"RNA-binding 2"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 30 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 48 |
| Details | Binding site: {} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 6 |
| Details | Site: {"description":"RNA-binding 2"} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1ohh |
| Chain | Residue | Details |
| A | ARG366 |
| site_id | CSA10 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ohh |
| Chain | Residue | Details |
| D | ARG212 | |
| D | GLU211 | |
| D | LYS184 |
| site_id | CSA11 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ohh |
| Chain | Residue | Details |
| E | ARG212 | |
| E | GLU211 | |
| E | LYS184 |
| site_id | CSA12 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ohh |
| Chain | Residue | Details |
| F | ARG212 | |
| F | GLU211 | |
| F | LYS184 |
| site_id | CSA2 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1ohh |
| Chain | Residue | Details |
| B | ARG366 |
| site_id | CSA3 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1ohh |
| Chain | Residue | Details |
| C | ARG366 |
| site_id | CSA4 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1ohh |
| Chain | Residue | Details |
| D | ARG366 |
| site_id | CSA5 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1ohh |
| Chain | Residue | Details |
| E | ARG366 |
| site_id | CSA6 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1ohh |
| Chain | Residue | Details |
| F | ARG366 |
| site_id | CSA7 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ohh |
| Chain | Residue | Details |
| A | ARG212 | |
| A | GLU211 | |
| A | LYS184 |
| site_id | CSA8 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ohh |
| Chain | Residue | Details |
| B | ARG212 | |
| B | GLU211 | |
| B | LYS184 |
| site_id | CSA9 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ohh |
| Chain | Residue | Details |
| C | ARG212 | |
| C | GLU211 | |
| C | LYS184 |






