PPIRE03099
Target Protein Information
| Protein_Name | General transcription factor IIH subunit 1 |
|---|---|
| Protein_Sequence | MATSSEEVLLIVKKVRQKKQDGALYLMAERIAWAPEGKDRFTISHMYADIKCQKISPEGKAKIQLQLVLHAGDTTNFHFSNESTAVKERDAVKDLLQQLLPKFKRKANKELEEKNRMLQEDPVLFQLYKDLVVSQVISAEEFWANRLNVNATDSSSTSNHKQDVGISAAFLADVRPQTDGCNGLRYNLTSDIIESIFRTYPAVKMKYAENVPHNMTEKEFWTRFFQSHYFHRDRLNTGSKDLFAECAKIDEKGLKTMVSLGVKNPLLDLTALEDKPLDEGYGISSVPSASNSKSIKENSNAAIIKRFNHHSAMVLAAGLRKQEAQNEQTSEPSNMDGNSGDADCFQPAVKRAKLQESIEYEDLGKNNSVKTIALNLKKSDRYYHGPTPIQSLQYATSQDIINSFQSIRQEMEAYTPKLTQVLSSSAASSTITALSPGGALMQGGTQQAINQMVPNDIQSELKHLYVAVGELLRHFWSCFPVNTPFLEEKVVKMKSNLERFQVTKLCPFQEKIRRQYLSTNLVSHIEEMLQTAYNKLHTWQSRRLMKKT |
| Organism_Source | Homo sapiens |
| Functional_Classification | Transcriptional regulator |
| Cellular_Localization | Nucleus |
| Gene_Names | GTF2H1 |
| UniProt_ID | P32780 |
| Protein-Protein Interaction Networks | |
Peptide Basic Information
| Peptide_Name | XPC124-142 L139A |
|---|---|
| Peptide_Sequence | EEEEESENDWEEVEEASEP |
| Peptide_Length | 19 |
| Peptide_SMILES | CC(C)[C@H](NC(=O)[C@H](CCC(=O)O)NC(=O)[C@H](CCC(=O)O)NC(=O)[C@H](Cc1c[nH]c2ccccc12)NC(=O)[C@H](CC(=O)O)NC(=O)[C@H](CC(N)=O)NC(=O)[C@H](CCC(=O)O)NC(=O)[C@H](CO)NC(=O)[C@H](CCC(=O)O)NC(=O)[C@H](CCC(=O)O)NC(=O)[C@H](CCC(=O)O)NC(=O)[C@H](CCC(=O)O)NC(=O)[C@@H](N)CCC(=O)O)C(=O)N[C@@H](CCC(=O)O)C(=O)N[C@@H](CCC(=O)O)C(=O)N[C@@H](C)C(=O)N[C@@H](CO)C(=O)N[C@@H](CCC(=O)O)C(=O)N1CCC[C@H]1C(=O)O |
| Chemical_Modification | None |
| Cyclization_Method | None |
| Linear/Cyclic | Linear |
| N-terminal_Modification | Free |
| C-terminal_Modification | Free |
| Amino_Acid_Distribution | |
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Peptide Physicochemical
| Molecular_Weight | 2295.18 |
|---|---|
| Aliphatic_Index | 20.52632 |
| Aromaticity | 0.05263 |
| Average_Rotatable_Bonds | 4.10526 |
| Charge_at_pH_7 | -11.98204 |
| Isoelectric_Point | 2.94475 |
|---|---|
| Number_of_Hydrogen_Bond_Acceptors | 35 |
| Number_of_Hydrogen_Bond_Donors | 35 |
| Topological_Polar_Surface_Area | 1125.27000 |
| X_logP_energy | -12.12170 |
Interaction Information
| Affinity | KD=77.5 nM |
|---|---|
| Affinity_Assay | Isothermal titration calorimetry |
| PDB_ID | None |
| Type | Affinity ligand |
| Structure | |
Reference Information
| Document_Type | Research Articles |
|---|---|
| Title | Structural Insight into the Mechanism of TFIIH Recognition by the Acidic String of the Nucleotide Excision Repair Factor XPC. |
| Release_Year | 2015 |
| PMID | 26278177 |
| DOI | 10.1016/j.str.2015.07.009 |