Research workbench
Crystal structure of human tyrosine-protein kinase C-src
Analyse Crystal structure of human tyrosine-protein kinase C-src in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1FMK
- Type
- protein
- Length
- 438 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Tyrosine-protein kinase src
- EC
- 2.7.1.112
- UniProt
- P12931
- Pockets
- 4 · best druggability 0.72
Structure
x-ray diffraction · 1 distinct chain · 29% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Tyrosine-protein kinase src (EC 2.7.1.112) | protein | 438 | 29% helix, 23% strand | P12931 |
Pockets
4 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 291 | 0.72 | 0.85 | 42 | empty |
| 2 | 1049 | 0.72 | 0.76 | 79 | empty |
| 3 | 272 | 0.52 | 0.75 | 34 | empty |
| 4 | 75 | 0.35 | 0.76 | 17 | empty |
Modifications
Observed in the structure: 1 modified (phosphorylation).
Compared structures
- 1FMK · Crystal structure of human tyrosine-protein kinase C-src · 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 1FMK · PDBe 1FMK · UniProt P12931
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