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Crystal structure of the human fyn SH3 domain

Analyse Crystal structure of the human fyn SH3 domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3UA6
Type
protein
Length
117 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, 44% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ATyrosine-protein kinase fyn (EC 2.7.10.2)protein575% helix, 47% strandP06241
BTyrosine-protein kinase fyn (EC 2.7.10.2)protein605% helix, 40% strandP06241

Ligands and binding sites

  • NA · Sodium ion · metal · 3 copies · chains A, B
  • FMT · Formic acid · additive · 6 copies · chains A, B
  • GOL · Glycerol · additive · 2 copies · chains A, B

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Interfaces

1 interface between chains.

  • A–B · 327 Ų buried · 4 hydrogen bonds · protein-protein

Compared structures

  • 3UA6 · Crystal Structure of the Human Fyn SH3 domain · 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

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