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Crystal structure of anti-muscle specific kinase (musk) Fab, MUSK1B

Analyse Crystal structure of anti-muscle specific kinase (musk) Fab, MUSK1B in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6WYT
Type
protein
Length
429 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
MUSK1B heavy chain; MUSK1B light chain
Ligands
NAG
Pockets
4 · best druggability 0.63

Structure

x-ray diffraction · 2 distinct chains · 7% helix, 50% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
HMUSK1B heavy chainprotein2205% helix, 49% strand—
LMUSK1B light chainprotein2098% helix, 51% strand—

Ligands and binding sites

  • NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · chains L
  • GOL · Glycerol · additive · 3 copies · chains H, L

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
15790.630.7559empty
21630.530.8028empty
3820.400.7817empty
4500.250.7315empty

Interfaces

1 interface between chains.

  • H–L · 1714 Ų buried · 18 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 4 disulfide, 1 glycan (disulfide, N-glycosylation).

Compared structures

  • 6WYT · Crystal structure of anti-Muscle Specific Kinase (MuSK) Fab, MuSK1B · the same entry in another collection · chain H against H, TM-score 1.00

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