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Crystal structure of human SLITRK1

Analyse Crystal structure of human SLITRK1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
4RCW
Type
protein
Length
466 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Slit and ntrk-like protein 1
UniProt
Q96PX8
Pockets
5 · best druggability 0.83

Structure

x-ray diffraction · 2 distinct chains · 13% helix, 20% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ASlit and ntrk-like protein 1protein23413% helix, 20% strandQ96PX8
BSlit and ntrk-like protein 1protein23213% helix, 20% strandQ96PX8

Pockets

5 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
16260.830.8882empty
27850.690.7677empty
3760.530.8517empty
4680.410.8015empty
5560.310.7616empty

Interfaces

1 interface between chains.

  • A–B · 1509 Ų buried · 20 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 6 disulfide (disulfide).

Compared structures

  • 4RCW · Crystal structure of human Slitrk1 · the same entry in another collection · chain A against A, TM-score 1.00
  • Q96PX8 · AlphaFold monomer V2.0 prediction for slit and ntrk-like protein 1 (Q96PX8) · a predicted model of the same protein · chain A against A, TM-score 0.97

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