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Structural evidence for antigen receptor evolution

Analyse Structural evidence for antigen receptor evolution in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
4N1C
Type
protein
Length
330 residues
Chains
3
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Immunoglobulin variable light chain domain; Lysozyme C
EC
3.2.1.17
UniProt
P00698
Pockets
4 · best druggability 0.72

Structure

x-ray diffraction · 3 distinct chains · 17% helix, 36% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AImmunoglobulin variable light chain domainprotein1073% helix, 50% strand—
BImmunoglobulin variable light chain domainprotein1063% helix, 49% strand—
CLysozyme C (EC 3.2.1.17)protein11744% helix, 10% strandP00698

Pockets

4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1660.720.9721empty
2870.560.8617empty
3610.320.7612empty
4580.260.7318empty

Interfaces

3 interfaces between chains.

  • A–B · 734 Ų buried · 14 hydrogen bonds · protein-protein
  • B–C · 431 Ų buried · 7 hydrogen bonds · protein-protein
  • A–C · 310 Ų buried · 6 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 6 disulfide (disulfide).

Compared structures

  • 4N1C · Structural evidence for antigen receptor evolution · the same entry in another collection · chain A against A, TM-score 1.00

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