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Crystal structure analysis of an anti-lysozyme antibody

Analyse Crystal structure analysis of an anti-lysozyme antibody in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1P2C
Type
protein
Length
1,102 residues
Chains
6
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Light chain anti-lysozyme antibody F10.6.6; Heavy chain VH+CH1 anti-lysozyme antibody…
EC
3.2.1.17
UniProt
P00698
Pockets
6 · best druggability 0.62

Structure

x-ray diffraction · 5 distinct chains · 11% helix, 47% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ALight chain anti-lysozyme antibody F10.6.6protein2127% helix, 51% strand—
BHeavy chain VH+CH1 anti-lysozyme antibody F10.6.6protein2106% helix, 53% strand—
C, FLysozyme C (EC 3.2.1.17)protein12940% helix, 11% strandP00698
DLight chain anti-lysozyme antibody F10.6.6protein2117% helix, 51% strand—
EHeavy chain VH+CH1 anti-lysozyme antibody F10.6.6protein2117% helix, 54% strand—

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
16020.620.7462empty
25920.610.7467empty
3860.340.7418empty
4810.330.7419empty
5600.300.7516empty

Interfaces

7 interfaces between chains.

  • A–B · 1804 Ų buried · 19 hydrogen bonds · protein-protein
  • D–E · 1783 Ų buried · 13 hydrogen bonds · protein-protein
  • E–F · 537 Ų buried · 8 hydrogen bonds · protein-protein
  • B–C · 522 Ų buried · 11 hydrogen bonds · protein-protein
  • D–F · 315 Ų buried · 3 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 16 disulfide (disulfide).

Compared structures

  • 1P2C · crystal structure analysis of an anti-lysozyme antibody · the same entry in another collection · chain A against A, TM-score 1.00

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