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Application of anti-helix antibodies in protein structure determination (8188-3LRH)

Analyse Application of anti-helix antibodies in protein structure determination… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6K64
Type
protein
Length
330 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
3LRH intrabody; Protein a
Pockets
4 · best druggability 0.67

Structure

x-ray diffraction · 2 distinct chains · 30% helix, 34% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B3LRH intrabodyprotein1093% helix, 51% strand—
H, CProtein aprotein5684% helix, 0% strand—

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
14400.670.7935empty
21910.480.7624empty
31990.470.7528empty
4510.320.7711empty

Interfaces

4 interfaces between chains.

  • B–H · 660 Ų buried · 1 hydrogen bond · protein-protein
  • A–C · 660 Ų buried · 1 hydrogen bond · protein-protein
  • A–B · 362 Ų buried · 7 hydrogen bonds · protein-protein
  • B–C · 258 Ų buried · 3 hydrogen bonds · protein-protein

Compared structures

  • 6K64 · Application of anti-helix antibodies in protein structure determination (8188-3LRH) · the same entry in another collection · chain A against A, TM-score 1.00

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