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The structure of an antitumor CH2-domain-deleted humanized antibody

Analyse The structure of an antitumor CH2-domain-deleted humanized antibody in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1ZA6
Type
protein
Length
2,176 residues
Chains
8
Method
x-ray diffraction
Collection
MolNFT v2 / PDB Bank
Contract
0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner
0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution
2.8
Source
Homo sapiens
Molecule
IGG Light chain; IGG Heavy chain
UniProt
Q6GMV9, Q6GMX6
Pockets
20 · best druggability 0.72

Structure

x-ray diffraction · resolution 2.8 · 2 distinct chains · 6% helix, 50% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, C, E, GIGG Light chainprotein2207% helix, 50% strandQ6GMV9
B, D, F, HIGG Heavy chainprotein3246% helix, 50% strandQ6GMX6

Pockets

20 pockets found on a 1 Å grid, 14 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
111220.720.76138empty
26960.700.7877empty
33750.700.8239empty
43330.690.8331empty
52720.610.8036empty

Interfaces

16 interfaces between chains.

  • E–F · 1809 Ų buried · 14 hydrogen bonds · protein-protein
  • G–H · 1746 Ų buried · 9 hydrogen bonds · protein-protein
  • A–B · 1728 Ų buried · 10 hydrogen bonds · protein-protein
  • C–D · 1706 Ų buried · 10 hydrogen bonds · protein-protein
  • F–H · 1372 Ų buried · 22 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 24 disulfide (disulfide).

Compared structures

  • 1ZA6 · The structure of an antitumor CH2-domain-deleted humanized antibody · the same entry in another collection · chain A against A, TM-score 1.00

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