Function and Biology Details
Biochemical function:
Biological process:
Cellular component:
Structure analysis Details
Assembly composition:
hetero trimer (preferred)
Assembly name:
Barrier-to-autointegration factor and Emerin (preferred)
PDBe Complex ID:
PDB-CPX-131039 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Barrier-to-autointegration factor
Molecule details ›
Chains: A, B
Length: 89 amino acids
Theoretical weight: 10.07 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
Sequence domains: Barrier to autointegration factor
Structure domains: Barrier-to-autointegration factor, BAF
Length: 89 amino acids
Theoretical weight: 10.07 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
- Canonical:
O75531 (Residues: 1-89; Coverage: 100%)
Sequence domains: Barrier to autointegration factor
Structure domains: Barrier-to-autointegration factor, BAF
Emerin
Molecule details ›
Chain: C
Length: 47 amino acids
Theoretical weight: 5.72 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
Sequence domains: LEM domain
Structure domains: Transcription Termination Factor Rho, Rna-binding Domain; Chain A, Domain 1
Length: 47 amino acids
Theoretical weight: 5.72 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
- Canonical: P50402 (Residues: 2-47; Coverage: 18%)
Sequence domains: LEM domain
Structure domains: Transcription Termination Factor Rho, Rna-binding Domain; Chain A, Domain 1
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
Refinement method:
CONJOINED RIGID BODY/TORSION ANGLE SIMULATED ANNEALING DYNAMICS
Expression system: Escherichia coli
