Research workbench
Conserved hydrophobic clusters on the surface of the CAF1A usher C-terminal domain are important for F1 antigen assembly
Analyse Conserved hydrophobic clusters on the surface of the CAF1A usher C-terminal… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2XET
- Type
- protein
- Length
- 177 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- F1 capsule-anchoring protein
- UniProt
- P26949
- Ligands
- SO4
- Pockets
- 2 · best druggability 0.37
Structure
x-ray diffraction · 2 distinct chains · 0% helix, 49% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | F1 capsule-anchoring protein | protein | 89 | 0% helix, 52% strand | P26949 |
| B | F1 capsule-anchoring protein | protein | 88 | 0% helix, 47% strand | P26949 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 3 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 98 | 0.37 | 0.75 | 19 | empty |
| 2 | 59 | 0.26 | 0.73 | 13 | empty |
Interfaces
1 interface between chains.
- A–B · 539 Ų buried · 10 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
- 2XET · Conserved hydrophobic clusters on the surface of the Caf1A usher C-terminal domain are… · the same entry in another collection · chain A against A, TM-score 1.00
- P26949 · AlphaFold monomer V2.0 prediction for F1 capsule-anchoring protein (P26949) · a predicted model of the same protein · chain B against A, TM-score 0.88
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 P26949
- Elsewhere: RCSB PDB 2XET · PDBe 2XET · UniProt P26949
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