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Unusual twinning in crystals of the cits binding antibody Fab fragment F3P4

Analyse Unusual twinning in crystals of the cits binding antibody Fab fragment F3P4 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2V7N
Type
protein
Length
1,700 residues
Chains
8
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Immunoglobulin light chain; Immunoglobulin heavy chain
Pockets
19 · best druggability 0.66

Structure

x-ray diffraction · 6 distinct chains · 9% helix, 52% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, EImmunoglobulin light chainprotein2137% helix, 51% strand—
BImmunoglobulin heavy chainprotein21410% helix, 52% strand—
C, GImmunoglobulin light chainprotein2127% helix, 50% strand—
DImmunoglobulin heavy chainprotein2138% helix, 53% strand—
FImmunoglobulin heavy chainprotein21210% helix, 52% strand—
HImmunoglobulin heavy chainprotein21110% helix, 53% strand—

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
16600.660.7649empty
2600.560.8921empty
33840.560.7434empty
43340.530.7450empty
53300.530.7432empty

Interfaces

10 interfaces between chains.

  • E–F · 1647 Ų buried · 15 hydrogen bonds · protein-protein
  • A–B · 1637 Ų buried · 15 hydrogen bonds · protein-protein
  • G–H · 1614 Ų buried · 13 hydrogen bonds · protein-protein
  • C–D · 1613 Ų buried · 13 hydrogen bonds · protein-protein
  • D–G · 275 Ų buried · 3 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 16 disulfide (disulfide).

Compared structures

  • 2V7N · Unusual twinning in crystals of the CitS binding antibody Fab fragment f3p4 · the same entry in another collection · chain A against A, TM-score 1.00

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