Research workbench
The crystal structure of human barrier-to-autointegration factor (baf)
Analyse The crystal structure of human barrier-to-autointegration factor (baf) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1CI4
- Type
- protein
- Length
- 177 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein (barrier-to-autointegration factor (baf))
- UniProt
- O75531
Structure
x-ray diffraction · 2 distinct chains · 67% helix, 1% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein (barrier-to-autointegration factor (baf)) | protein | 89 | 66% helix, 0% strand | O75531 |
| B | Protein (barrier-to-autointegration factor (baf)) | protein | 88 | 67% helix, 2% strand | O75531 |
Interfaces
1 interface between chains.
- A–B · 761 Ų buried · 7 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 3 modified (engineered).
Compared structures
- 1CI4 · The crystal structure of human barrier-to-autointegration factor (baf) · the same entry in another collection · chain A against A, TM-score 1.00
- O75531 · AlphaFold monomer V2.0 prediction for barrier-to-autointegration factor (O75531) · a predicted model of the same protein · chain B against A, TM-score 0.98
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt O75531
- Elsewhere: RCSB PDB 1CI4 · PDBe 1CI4 · UniProt O75531
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