MolNFT v1 · #28777 · protein
Crystal structure of src kinase domain
1YOJ · Proto-oncogene tyrosine-protein kinase src: “Crystal structure of src kinase domain”. X-ray diffraction, 5 pockets (best druggability 0.65). MolNFT v1 #28777 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1YOJ
- Type
- protein
- Length
- 448 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Proto-oncogene tyrosine-protein kinase src
- EC
- 2.7.1.112
- UniProt
- P12931
- Pockets
- 5 · best druggability 0.65
Structure
x-ray diffraction · 2 distinct chains · 43% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Proto-oncogene tyrosine-protein kinase src (EC 2.7.1.112) | protein | 233 | 42% helix, 17% strand | P12931 |
| B | Proto-oncogene tyrosine-protein kinase src (EC 2.7.1.112) | protein | 215 | 44% helix, 10% strand | P12931 |
Pockets
5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 481 | 0.65 | 0.77 | 51 | empty |
| 2 | 292 | 0.58 | 0.77 | 28 | empty |
| 3 | 193 | 0.47 | 0.75 | 30 | empty |
| 4 | 155 | 0.44 | 0.75 | 35 | empty |
| 5 | 77 | 0.36 | 0.76 | 13 | empty |
Interfaces
1 interface between chains.
- A–B · 379 Ų buried · 5 hydrogen bonds · protein-protein
Compared structures
- 1YOJ · Crystal structure of Src kinase domain · 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 P12931
- Elsewhere: RCSB PDB 1YOJ · PDBe 1YOJ · UniProt P12931
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.