Transcription termination factor Rho (P0AG30)
Annotations
This section shows residue-level functional annotations available for the PDB entries related to this protein. These annotations are contributed by members of the PDBe-KB consortium or generated by weekly data pipelines. For more information see the PDBe-KB Wiki pages.
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Annotated Residues
The visualisation is using UniProt numbering for residues, not PDB numbering.
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Curated metal binding sites | |
Curated interface annotations | |
Predicted ligand binding sites | |
Molecular channels | |
Biophysical parameters | |
Domains | |
Ligand binding sites | |
Interaction interfaces | |
Sequence conservation | |
Curated metal binding sites
MetalPDB is a database of metal sites in biological macromolecular structures
Curated interface annotations
3D Complex is a hierarchical classification of protein complexes that describes similarities in structure, sequence, as well as topology of contacts of the constituent proteins
Predicted ligand binding sites
3DLigandSite is an automated method for the prediction of ligand binding sites
P2Rank is a new open source software package for ligand binding site prediction from protein structure
Molecular channels
ChannelsDB is a database providing information about the positions, geometry and physicochemical properties of channels (pores and tunnels) found within biomacromolecular structures deposited in the Protein Data Bank
Biophysical parameters
POPSCOMP is a method to analyse interactions between individual complex components of proteins and/or nucleic acids by calculating the solvent accessible surface area (SASA) buried upon complex formation.
POPSCOMP is a method to analyse interactions between individual complex components of proteins and/or nucleic acids by calculating the solvent accessible surface area (SASA) buried upon complex formation.
POPSCOMP is a method to analyse interactions between individual complex components of proteins and/or nucleic acids by calculating the solvent accessible surface area (SASA) buried upon complex formation.
3D Complex is a hierarchical classification of protein complexes that describes similarities in structure, sequence, as well as topology of contacts of the constituent proteins
3D Complex is a hierarchical classification of protein complexes that describes similarities in structure, sequence, as well as topology of contacts of the constituent proteins
Domains
Residues mapped to CATH domains
Residues mapped to SCOP domains
Residues mapped to InterPro domains
Ligand binding sites
Residues binding ADENOSINE-5'-DIPHOSPHATE<br><span style="display:inline-block;width:100%;text-align:center;margin-top:5px;"><img src="https://www.ebi.ac.uk/pdbe/static/files/pdbechem_v2/ADP_200.svg" /><span>
Residues binding ADENOSINE-5'-TRIPHOSPHATE<br><span style="display:inline-block;width:100%;text-align:center;margin-top:5px;"><img src="https://www.ebi.ac.uk/pdbe/static/files/pdbechem_v2/ATP_200.svg" /><span>
Residues binding PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER<br><span style="display:inline-block;width:100%;text-align:center;margin-top:5px;"><img src="https://www.ebi.ac.uk/pdbe/static/files/pdbechem_v2/ANP_200.svg" /><span>
Residues binding PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER<br><span style="display:inline-block;width:100%;text-align:center;margin-top:5px;"><img src="https://www.ebi.ac.uk/pdbe/static/files/pdbechem_v2/AGS_200.svg" /><span>
Residues binding THYMIDINE-5'-MONOPHOSPHATE<br><span style="display:inline-block;width:100%;text-align:center;margin-top:5px;"><img src="https://www.ebi.ac.uk/pdbe/static/files/pdbechem_v2/DT_200.svg" /><span>
Residues binding 2'-DEOXYGUANOSINE-5'-MONOPHOSPHATE<br><span style="display:inline-block;width:100%;text-align:center;margin-top:5px;"><img src="https://www.ebi.ac.uk/pdbe/static/files/pdbechem_v2/DG_200.svg" /><span>
Residues binding guanosine 5'-(tetrahydrogen triphosphate) 3'-(trihydrogen diphosphate)<br><span style="display:inline-block;width:100%;text-align:center;margin-top:5px;"><img src="https://www.ebi.ac.uk/pdbe/static/files/pdbechem_v2/0O2_200.svg" /><span>
Residues binding 5A-(3-FORMYLPHENYLSULFANYL)-DIHYDROBICYCLOMYCIN<br><span style="display:inline-block;width:100%;text-align:center;margin-top:5px;"><img src="https://www.ebi.ac.uk/pdbe/static/files/pdbechem_v2/FPD_200.svg" /><span>
Residues binding BICYCLOMYCIN<br><span style="display:inline-block;width:100%;text-align:center;margin-top:5px;"><img src="https://www.ebi.ac.uk/pdbe/static/files/pdbechem_v2/BCM_200.svg" /><span>
Residues binding 5A-FORMYLBICYCLOMYCIN<br><span style="display:inline-block;width:100%;text-align:center;margin-top:5px;"><img src="https://www.ebi.ac.uk/pdbe/static/files/pdbechem_v2/FB_200.svg" /><span>
Residues binding SPERMIDINE<br><span style="display:inline-block;width:100%;text-align:center;margin-top:5px;"><img src="https://www.ebi.ac.uk/pdbe/static/files/pdbechem_v2/SPD_200.svg" /><span>
Residues binding SULFATE ION<br><span style="display:inline-block;width:100%;text-align:center;margin-top:5px;"><img src="https://www.ebi.ac.uk/pdbe/static/files/pdbechem_v2/SO4_200.svg" /><span>
Residues binding (4S)-2-METHYL-2,4-PENTANEDIOL<br><span style="display:inline-block;width:100%;text-align:center;margin-top:5px;"><img src="https://www.ebi.ac.uk/pdbe/static/files/pdbechem_v2/MPD_200.svg" /><span>
Residues binding MAGNESIUM ION<br><span style="display:inline-block;width:100%;text-align:center;margin-top:5px;"><img src="https://www.ebi.ac.uk/pdbe/static/files/pdbechem_v2/MG_200.svg" /><span>
Residues binding BERYLLIUM TRIFLUORIDE ION<br><span style="display:inline-block;width:100%;text-align:center;margin-top:5px;"><img src="https://www.ebi.ac.uk/pdbe/static/files/pdbechem_v2/BEF_200.svg" /><span>
Interaction interfaces
Residues interacting with Transcription termination factor Rho (self) (P0AG30)
Residues interacting with Polarity suppression protein (P05460)
Residues interacting with RNA (RNA)
Residues interacting with Transcription termination/antitermination protein NusA (P0AFF6)
Residues interacting with DNA (DNA)
Residues interacting with Transcription termination/antitermination protein NusG (P0AFG0)
Residues interacting with DNA-directed RNA polymerase subunit beta (P0A8V2)
Residues interacting with Protein rof (P0AFW8)
Residues interacting with DNA-directed RNA polymerase subunit beta' (P0A8T7)
Residues interacting with DNA-directed RNA polymerase subunit alpha (P0A7Z4)
Sequence conservation
Amino acid probabilities
The amino acid probabilities are calculated using HMM profiles based on multiple sequence alignments. Click to see more details...
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Amino acid properties
Aromatic
Polar
Hydrophobic
Negative charge
Proline
Positive charge
Cysteine
Glycine
Variants
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Annotations :
Predicted annotations
Curated annotations
Domains :
CATH domains
SCOP domains
InterPro annotations