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Crystal structure of fv polyglutamine complex

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

PDB
2OTU
Type
protein
Length
976 residues
Chains
12
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Fv light chain variable domain; Fv heavy chain variable domain; Peptide antigen
UniProt
A2NN81
Pockets
8 · best druggability 0.83

Structure

x-ray diffraction · 3 distinct chains · 6% helix, 50% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, C, E, GFv light chain variable domainprotein1155% helix, 49% strand—
B, D, F, HFv heavy chain variable domainprotein1188% helix, 54% strandA2NN81
P, Q, R, SPeptide antigenprotein110% helix, 9% strand—

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
110450.830.8494empty
211540.780.8096empty
33800.630.7858empty
41390.430.7527empty
51370.410.7420empty

Interfaces

27 interfaces between chains.

  • C–D · 952 Ų buried · 6 hydrogen bonds · protein-protein
  • A–B · 948 Ų buried · 7 hydrogen bonds · protein-protein
  • G–H · 926 Ų buried · 6 hydrogen bonds · protein-protein
  • E–F · 909 Ų buried · 7 hydrogen bonds · protein-protein
  • B–D · 531 Ų buried · 2 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 8 disulfide (disulfide).

Compared structures

  • 2OTU · Crystal structure of Fv polyglutamine complex · the same entry in another collection · chain A against A, TM-score 1.00

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