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Antibody structural organization: role of kappa - lambda chain constant domain switch in catalytic functionality

Analyse Antibody structural organization: role of kappa - lambda chain constant domain… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3ZL4
Type
protein
Length
445 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
A17 antibody Fab fragment heavy chain; A17 antibody Fab fragment lambda light chain
Pockets
5 · best druggability 0.78

Structure

x-ray diffraction · 2 distinct chains · 6% helix, 48% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
HA17 antibody Fab fragment heavy chainprotein2317% helix, 48% strand—
LA17 antibody Fab fragment lambda light chainprotein2146% helix, 49% strand—

Ligands and binding sites

  • MES · 2-(N-morpholino)-ethanesulfonic acid · additive · chains H, L

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1980.780.9819MES
21790.560.8031empty
34010.530.7345empty
41120.430.7723empty
5850.320.7319empty

Interfaces

1 interface between chains.

  • H–L · 1921 Ų buried · 23 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 5 disulfide (disulfide).

Compared structures

  • 3ZL4 · Antibody structural organization: Role of kappa - lambda chain constant domain switch in… · the same entry in another collection · chain H against H, TM-score 1.00

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