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Crystal structure of the apo SH2 domains of syk

Analyse Crystal structure of the apo SH2 domains of syk in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7SA7
Type
protein
Length
1,427 residues
Chains
6
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Tyrosine-protein kinase syk
EC
2.7.10.2
UniProt
P43405
Pockets
20 · best druggability 0.70

Structure

x-ray diffraction · 5 distinct chains · 24% helix, 26% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ATyrosine-protein kinase syk (EC 2.7.10.2)protein22121% helix, 28% strandP43405
BTyrosine-protein kinase syk (EC 2.7.10.2)protein23625% helix, 25% strandP43405
CTyrosine-protein kinase syk (EC 2.7.10.2)protein21820% helix, 27% strandP43405
DTyrosine-protein kinase syk (EC 2.7.10.2)protein24423% helix, 25% strandP43405
E, FTyrosine-protein kinase syk (EC 2.7.10.2)protein25428% helix, 24% strandP43405

Pockets

20 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
15670.700.7957empty
23140.650.8149empty
32440.640.8236empty
44460.640.7750empty
51350.580.8425empty

Interfaces

7 interfaces between chains.

  • D–F · 465 Ų buried · 1 hydrogen bond · protein-protein
  • A–F · 207 Ų buried · 1 hydrogen bond · protein-protein
  • A–D · 189 Ų buried · 2 hydrogen bonds · protein-protein
  • B–E · 66 Ų buried · 0 hydrogen bonds · protein-protein
  • B–C · 65 Ų buried · 0 hydrogen bonds · protein-protein

Compared structures

  • 7SA7 · Crystal structure of the apo SH2 domains of Syk · the same entry in another collection · chain A against A, TM-score 1.00

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