MolNFT v1 · #18302 · protein
Structure of a C-kit kinase product complex
1PKG · C-kit protein: “Structure of a C-kit kinase product complex”. X-ray diffraction, 2 ligands (ADP, MG), 5 pockets (best druggability 0.70). MolNFT v1 #18302 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1PKG
- Type
- protein
- Length
- 571 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- C-kit protein
- UniProt
- P10721
- Ligands
- ADP, MG
- Pockets
- 5 · best druggability 0.70
Structure
x-ray diffraction · 2 distinct chains · 38% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | C-kit protein | protein | 292 | 38% helix, 18% strand | P10721 |
| B | C-kit protein | protein | 279 | 38% helix, 16% strand | — |
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
5 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 183 | 0.70 | 0.88 | 31 | MG, ADP |
| 2 | 217 | 0.69 | 0.86 | 33 | MG, ADP |
| 3 | 493 | 0.63 | 0.76 | 48 | empty |
| 4 | 202 | 0.51 | 0.77 | 39 | empty |
| 5 | 121 | 0.43 | 0.76 | 26 | empty |
Interfaces
1 interface between chains.
- A–B · 992 Ų buried · 16 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 modified (phosphorylation).
Compared structures
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 P10721
- Elsewhere: RCSB PDB 1PKG · PDBe 1PKG · UniProt P10721
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