Research workbench
Crystal structure of the chimerical protein capab
Analyse Crystal structure of the chimerical protein capab in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3BFV
- Type
- protein
- Length
- 482 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Membrane protein CAPA1, protein tyrosine KINASE,PROTEIN tyrosine kinase
- UniProt
- P72367, A8YPQ5
- Ligands
- ADP, MG
- Pockets
- 4 · best druggability 0.50
Structure
x-ray diffraction · 1 distinct chain · 39% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Membrane protein CAPA1, protein tyrosine KINASE,PROTEIN tyrosine kinase | protein | 241 | 39% helix, 19% strand | P72367, A8YPQ5 |
Ligands and binding sites
- ADP · Adenosine-5'-diphosphate · ligand · 2 copies · chains A, B
- MG · Magnesium ion · metal · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 252 | 0.50 | 0.74 | 41 | empty |
| 2 | 175 | 0.44 | 0.74 | 21 | empty |
| 3 | 108 | 0.37 | 0.74 | 23 | MG, ADP |
| 4 | 97 | 0.35 | 0.74 | 23 | MG, ADP |
Interfaces
1 interface between chains.
- A–B · 358 Ų buried · 2 hydrogen bonds · protein-protein
Compared structures
- 3BFV · crystal structure of the chimerical protein CapAB · the same entry in another collection · chain A against A, TM-score 1.00
- P72367 · AlphaFold monomer V2.0 prediction for capsular polysaccharide type 8 biosynthesis protein… · a predicted model of the same protein · chain A against A, TM-score 0.20
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 P72367
- Every structure of UniProt A8YPQ5
- Elsewhere: RCSB PDB 3BFV · PDBe 3BFV · UniProt P72367 · UniProt A8YPQ5
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