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Complex structure of LILRB4 and H128-3 antibody

Analyse Complex structure of LILRB4 and H128-3 antibody in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6K7O
Type
protein
Length
2,148 residues
Chains
12
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Leukocyte immunoglobulin-like receptor subfamily B member 4; H128-3 Fab heavy chain…
UniProt
Q8NHJ6
Pockets
20 · best druggability 0.76

Structure

x-ray diffraction · 3 distinct chains · 6% helix, 50% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, P, R, QLeukocyte immunoglobulin-like receptor subfamily B member 4protein943% helix, 45% strandQ8NHJ6
B, D, F, HH128-3 Fab heavy chainprotein2257% helix, 51% strand—
C, E, G, LH128-3 Fab light chainprotein2187% helix, 50% strand—

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
110800.760.7891empty
24540.680.8057empty
34930.650.7754empty
44590.630.7755empty
54020.600.7649empty

Interfaces

24 interfaces between chains.

  • F–G · 2256 Ų buried · 14 hydrogen bonds · protein-protein
  • B–C · 2215 Ų buried · 18 hydrogen bonds · protein-protein
  • D–E · 2191 Ų buried · 21 hydrogen bonds · protein-protein
  • H–L · 2165 Ų buried · 16 hydrogen bonds · protein-protein
  • C–L · 915 Ų buried · 9 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 24 disulfide (disulfide).

Compared structures

  • 6K7O · Complex structure of LILRB4 and h128-3 antibody · the same entry in another collection · chain Q against Q, TM-score 1.00

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