MolNFT v1 · #107148 · protein
Swapped dimer of the human fyn-SH2 domain
4U17 · Tyrosine-protein kinase fyn: “Swapped dimer of the human fyn-SH2 domain”. X-ray diffraction, 1 ligand (PO4). MolNFT v1 #107148 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 4U17
- Type
- protein
- Length
- 308 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Tyrosine-protein kinase fyn
- EC
- 2.7.10.2
- UniProt
- P06241
- Ligands
- PO4
Structure
x-ray diffraction · 2 distinct chains · 17% helix, 35% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Tyrosine-protein kinase fyn (EC 2.7.10.2) | protein | 102 | 18% helix, 37% strand | P06241 |
| C | Tyrosine-protein kinase fyn (EC 2.7.10.2) | protein | 104 | 17% helix, 33% strand | P06241 |
Ligands and binding sites
- PO4 · Phosphate ion · ion · 7 copies · chains A, B, C
- EDO · 1,2-ethanediol · additive · 4 copies · chains A, C, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
2 interfaces between chains.
- A–C · 2429 Ų buried · 27 hydrogen bonds · protein-protein
- A–B · 241 Ų buried · 1 hydrogen bond · protein-protein
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 P06241
- Elsewhere: RCSB PDB 4U17 · PDBe 4U17 · UniProt P06241
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