Research workbench
Crystal structure of shka full-length in complex with amppnp
Analyse Crystal structure of shka full-length in complex with amppnp in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6QRJ
- Type
- protein
- Length
- 463 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Hybrid kinase
- UniProt
- Q9ABT2
- Ligands
- ANP, MG
- Pockets
- 4 · best druggability 0.74
Structure
x-ray diffraction · 1 distinct chain · 44% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Hybrid kinase | protein | 463 | 44% helix, 20% strand | Q9ABT2 |
Ligands and binding sites
- ANP · Phosphoaminophosphonic acid-adenylate ester · ligand · chains A
- MG · Magnesium ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 899 | 0.74 | 0.78 | 85 | ANP, MG |
| 2 | 161 | 0.46 | 0.76 | 26 | empty |
| 3 | 60 | 0.36 | 0.79 | 16 | empty |
| 4 | 67 | 0.28 | 0.74 | 16 | empty |
Compared structures
- 6QRJ · Crystal structure of ShkA full-length in complex with AMPPNP · 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 Q9ABT2
- Elsewhere: RCSB PDB 6QRJ · PDBe 6QRJ · UniProt Q9ABT2
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