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Structure of IGLB12 scfv in complex with anti-idiotype IB2 Fab

Analyse Structure of IGLB12 scfv in complex with anti-idiotype IB2 Fab in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6OL6
Type
protein
Length
668 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
IB2 heavy chain; IB2 light chain; IGLB12 heavy chain; IGLB12 light chain
Ligands
CL
Pockets
11 · best druggability 0.46

Structure

x-ray diffraction · 4 distinct chains · 7% helix, 51% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AIB2 heavy chainprotein2169% helix, 54% strand—
BIB2 light chainprotein2125% helix, 51% strand—
HIGLB12 heavy chainprotein12710% helix, 46% strand—
LIGLB12 light chainprotein1135% helix, 54% strand—

Ligands and binding sites

  • CL · Chloride ion · ion · 2 copies · chains A, H, L

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

Pockets

11 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11740.460.7533empty
21970.460.7425CL
31260.420.7624empty
4660.330.7616empty
5760.330.7520empty

Interfaces

4 interfaces between chains.

  • A–B · 1741 Ų buried · 15 hydrogen bonds · protein-protein
  • H–L · 945 Ų buried · 16 hydrogen bonds · protein-protein
  • A–H · 495 Ų buried · 12 hydrogen bonds · protein-protein
  • B–H · 259 Ų buried · 4 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 6 disulfide (disulfide).

Compared structures

  • 6OL6 · Structure of iglb12 scFv in complex with anti-idiotype ib2 Fab · the same entry in another collection · chain L against L, TM-score 1.00

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