Research workbench
Crystal structure of the chimerical protein CAPA1B1 in complex with ADP-mg
Analyse Crystal structure of the chimerical protein CAPA1B1 in complex with ADP-mg in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4JLV
- Type
- protein
- Length
- 228 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- C-terminal fragment of membrane protein CAPA1, putative uncharacterized protein CAPB1
- UniProt
- A8YPQ6, A8YPQ8
- Ligands
- ADP, MG
- Pockets
- 1 · best druggability 0.25
Structure
x-ray diffraction · 1 distinct chain · 40% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | C-terminal fragment of membrane protein CAPA1, putative uncharacterized protein CAPB1 | protein | 228 | 40% helix, 19% strand | A8YPQ6, A8YPQ8 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 54 | 0.25 | 0.72 | 19 | MG |
Compared structures
- 4JLV · Crystal structure of the chimerical protein CapA1B1 in complex with ADP-Mg · the same entry in another collection · chain A against A, TM-score 1.00
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 A8YPQ6
- Every structure of UniProt A8YPQ8
- Elsewhere: RCSB PDB 4JLV · PDBe 4JLV · UniProt A8YPQ6 · UniProt A8YPQ8
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