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Structure of mouse syndapin I (crystal form 1)

Analyse Structure of mouse syndapin I (crystal form 1) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2X3X
Type
protein
Length
968 residues
Chains
5
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Protein kinase C and casein kinase substrate in neurons protein 1
UniProt
Q61644
Pockets
8 · best druggability 0.59

Structure

x-ray diffraction · 3 distinct chains · 72% helix, 4% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, CProtein kinase C and casein kinase substrate in neurons protein 1protein29178% helix, 1% strandQ61644
BProtein kinase C and casein kinase substrate in neurons protein 1protein27478% helix, 1% strandQ61644
D, EProtein kinase C and casein kinase substrate in neurons protein 1protein565% helix, 41% strandQ61644

Pockets

8 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11850.590.8130empty
23650.580.7540empty
31150.370.7420empty
4810.350.7621empty
5550.340.7810empty

Interfaces

5 interfaces between chains.

  • A–B · 4875 Ų buried · 49 hydrogen bonds · protein-protein
  • A–D · 519 Ų buried · 10 hydrogen bonds · protein-protein
  • B–C · 388 Ų buried · 3 hydrogen bonds · protein-protein
  • A–E · 369 Ų buried · 6 hydrogen bonds · protein-protein
  • A–C · 328 Ų buried · 1 hydrogen bond · protein-protein

Compared structures

  • 2X3X · structure of mouse syndapin I (crystal form 1) · the same entry in another collection · chain E against E, TM-score 1.00
  • Q61644 · AlphaFold monomer V2.0 prediction for protein kinase C and casein kinase substrate in… · a predicted model of the same protein · chain A against A, TM-score 0.98

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