Research workbench
Crystal structure of the fyn SH3 domain mutant E129Q in space group C21 at pH 4.0
Analyse Crystal structure of the fyn SH3 domain mutant E129Q in space group C21 at pH… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7A2L
- Type
- protein
- Length
- 116 residues
- Chains
- 2
- 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
- NA
Structure
x-ray diffraction · 2 distinct chains · 5% helix, 43% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Tyrosine-protein kinase fyn (EC 2.7.10.2) | protein | 57 | 5% helix, 46% strand | P06241 |
| B | Tyrosine-protein kinase fyn (EC 2.7.10.2) | protein | 59 | 5% helix, 41% strand | P06241 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- A–B · 328 Ų buried · 5 hydrogen bonds · protein-protein
Compared structures
- 7A2L · Crystal structure of the Fyn SH3 domain mutant E129Q in space group C21 at pH 4.0 · the same entry in another collection · chain A against A, TM-score 1.00
- P06241 · AlphaFold monomer V2.0 prediction for tyrosine-protein kinase fyn (P06241) · a predicted model of the same protein · chain A against A, TM-score 0.95
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 7A2L · PDBe 7A2L · UniProt P06241
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