Aggregated Views of Proteins
Ubiquitin-like protein SMT3 (Q12306)
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 interface annotations | |
| Biophysical parameters | |
| Domains | |
| Ligand binding sites | |
| Interaction interfaces | |
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
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
Cospi-Depth is a server for computing/predicting depth, cavity sizes, ligand binding sites and pKa
Cospi-Depth is a server for computing/predicting depth, cavity sizes, ligand binding sites and pKa
Domains
Residues mapped to InterPro domains
Ligand binding sites
Residues binding IMIDAZOLE<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/IMD_200.svg" /><span>
Residues binding GLYCEROL<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/GOL_200.svg" /><span>
Residues binding FORMIC ACID<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/FMT_200.svg" /><span>
Residues binding CHLORIDE 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/CL_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 ethane-1,2-dithiol<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_v2/6LN_200.svg" /><span>
Residues binding BARIUM 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/BA_200.svg" /><span>
Interaction interfaces
Residues interacting with SUMO-conjugating enzyme UBC9 (P50623)
Residues interacting with Ubiquitin-like protein SMT3 (self) (Q12306)
Residues interacting with Ubiquitin-like-specific protease 1 (Q02724)
Residues interacting with E3 SUMO-protein ligase MMS21 (P38632)
Residues interacting with E3 SUMO-protein ligase SIZ1 (Q04195)
Residues interacting with Other
Residues interacting with Proliferating cell nuclear antigen (P15873)
Residues interacting with Trehalose synthase/amylase TreS (P9WQ19)
Residues interacting with ATP-dependent DNA helicase SRS2 (P12954)
Residues interacting with Long-chain-fatty-acid--AMP ligase FadD32 (A0R618)
Residues interacting with Stimulator of interferon genes protein (Q86WV6)
Residues interacting with Chromo domain-containing protein 1 (Q10103)
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
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Hydrophobic
Negative charge
Proline
Positive charge
Cysteine
Glycine
Variants
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Annotations :
Curated annotations
Domains :
InterPro annotations