Aggregated Views of Proteins
Endothelin-1 (P05305)
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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| Predicted ligand binding sites | |
| Biophysical parameters | |
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Predicted ligand binding sites
P2Rank is a new open source software package for ligand binding site prediction from protein structure
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 SCOP domains
Residues mapped to InterPro domains
Interaction interfaces
Residues interacting with Endothelin receptor type B (P24530)
Residues interacting with Endolysin (P00720)
Residues interacting with exo-alpha-sialidase (Q59310)
Residues interacting with Endothelin-1 receptor (P25101)
Residues interacting with Endothelin-1 (self) (P05305)
Residues interacting with Endoglucanase H (P16218)
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
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Hydrophobic
Negative charge
Proline
Positive charge
Cysteine
Glycine
Variants
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Annotations :
Predicted annotations
Domains :
SCOP domains
InterPro annotations