Function and Biology Details
Biochemical function:
- not assigned
Biological process:
- not assigned
Cellular component:
- not assigned
Sequence domains:
Structure domain:
Structure analysis Details
Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-528505 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
General transcription and DNA repair factor IIH subunit TFB1
Molecule details ›
Chain: A
Length: 115 amino acids
Theoretical weight: 12.9 KDa
Source organism: Saccharomyces cerevisiae S288C
Expression system: Escherichia coli
UniProt:
Sequence domains: TFIIH p62 subunit, N-terminal domain
Structure domains: Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB)
Length: 115 amino acids
Theoretical weight: 12.9 KDa
Source organism: Saccharomyces cerevisiae S288C
Expression system: Escherichia coli
UniProt:
- Canonical:
P32776 (Residues: 1-115; Coverage: 18%)
Sequence domains: TFIIH p62 subunit, N-terminal domain
Structure domains: Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB)
Tegument protein VP16
Molecule details ›
Chain: B
Length: 35 amino acids
Theoretical weight: 3.82 KDa
Source organism: Human alphaherpesvirus 1 strain F
Expression system: Escherichia coli
UniProt:
Sequence domains: Herpes simplex virus virion protein 16 C terminal
Length: 35 amino acids
Theoretical weight: 3.82 KDa
Source organism: Human alphaherpesvirus 1 strain F
Expression system: Escherichia coli
UniProt:
- Canonical: P04486 (Residues: 456-490; Coverage: 7%)
Sequence domains: Herpes simplex virus virion protein 16 C terminal
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
Refinement method:
simulated annealing, torsion angle dynamics, simulated annealing
Expression system: Escherichia coli
