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Application of anti-helix antibodies in protein structure determination (9011-3LRH)

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
6K67
Type
protein
Length
383 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
3LRH introbody; Engineered calmodulin
Ligands
CA
Pockets
3 · best druggability 0.45

Structure

x-ray diffraction · 3 distinct chains · 40% helix, 21% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, C3LRH introbodyprotein1093% helix, 49% strand—
BEngineered calmodulinprotein8365% helix, 2% strand—
DEngineered calmodulinprotein8265% helix, 2% strand—

Ligands and binding sites

  • CA · Calcium ion · metal · 4 copies · chains B, D

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12080.450.7333empty
2710.290.7217empty
3530.280.7413empty

Interfaces

3 interfaces between chains.

  • C–D · 673 Ų buried · 5 hydrogen bonds · protein-protein
  • A–B · 645 Ų buried · 5 hydrogen bonds · protein-protein
  • A–D · 358 Ų buried · 3 hydrogen bonds · protein-protein

Compared structures

  • 6K67 · Application of anti-helix antibodies in protein structure determination (9011-3LRH) · the same entry in another collection · chain A against A, TM-score 1.00

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