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Structure of the complex of antibody MN423 with a fragment of tau protein

Analyse Structure of the complex of antibody MN423 with a fragment of tau protein in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2V17
Type
protein
Length
442 residues
Chains
3
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Peptide fragment; Monoclonal antibody Fab fragment MN423
Pockets
5 · best druggability 0.60

Structure

x-ray diffraction · 3 distinct chains · 7% helix, 49% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
APeptide fragmentprotein60% helix, 0% strand—
HMonoclonal antibody Fab fragment MN423protein2227% helix, 51% strand—
LMonoclonal antibody Fab fragment MN423protein2147% helix, 49% strand—

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
15360.600.7467empty
21740.510.7824empty
3710.350.7717empty
4740.310.7418empty
5530.260.7314empty

Interfaces

3 interfaces between chains.

  • H–L · 1870 Ų buried · 14 hydrogen bonds · protein-protein
  • A–L · 243 Ų buried · 4 hydrogen bonds · protein-protein
  • A–H · 228 Ų buried · 4 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 4 disulfide (disulfide).

Compared structures

  • 2V17 · Structure of the complex of antibody MN423 with a fragment of tau protein · the same entry in another collection · chain A against A, TM-score 1.00

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