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The structure of the anti-C-myc antibody 9E10 Fab fragment

Analyse The structure of the anti-C-myc antibody 9E10 Fab fragment in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2ORB
Type
protein
Length
843 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Monoclonal anti-C-myc antibody 9E10
Ligands
SO4
Pockets
7 · best druggability 0.63

Structure

x-ray diffraction · 4 distinct chains · 5% helix, 52% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
LMonoclonal anti-C-myc antibody 9E10protein2125% helix, 52% strand—
HMonoclonal anti-C-myc antibody 9E10protein2126% helix, 52% strand—
MMonoclonal anti-C-myc antibody 9E10protein2105% helix, 52% strand—
IMonoclonal anti-C-myc antibody 9E10protein2096% helix, 51% strand—

Ligands and binding sites

  • SO4 · Sulfate ion · ion · 2 copies · chains H

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
15560.630.7554empty
25140.610.7553empty
33290.570.7643empty
41210.410.7624empty
51110.390.7528empty

Interfaces

3 interfaces between chains.

  • L–H · 1867 Ų buried · 11 hydrogen bonds · protein-protein
  • M–I · 1694 Ų buried · 9 hydrogen bonds · protein-protein
  • H–I · 232 Ų buried · 4 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 8 disulfide (disulfide).

Compared structures

  • 2ORB · The structure of the anti-c-myc antibody 9E10 Fab fragment · the same entry in another collection · chain L against L, TM-score 1.00

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