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Crystallographic refinement of the three-dimensional structure of the Fab D1.3-lysozyme complex at 2.5- ångströms resolution

Analyse Crystallographic refinement of the three-dimensional structure of the Fab… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1FDL
Type
protein
Length
561 residues
Chains
3
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
IGG1-kappa D1.3 Fab (light chain); IGG1-kappa D1.3 Fab (heavy chain); Hen egg white…
EC
3.2.1.17
UniProt
P00698
Pockets
7 · best druggability 0.69

Structure

x-ray diffraction · 3 distinct chains · 14% helix, 42% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
LIGG1-kappa D1.3 Fab (light chain)protein2146% helix, 50% strand—
HIGG1-kappa D1.3 Fab (heavy chain)protein2186% helix, 51% strand—
YHen egg white lysozyme (EC 3.2.1.17)protein12940% helix, 12% strandP00698

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1880.690.9318empty
22520.520.7533empty
32930.500.7340empty
4650.360.7816empty
5820.340.7517empty

Interfaces

3 interfaces between chains.

  • L–H · 1917 Ų buried · 26 hydrogen bonds · protein-protein
  • H–Y · 399 Ų buried · 12 hydrogen bonds · protein-protein
  • L–Y · 329 Ų buried · 4 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 9 disulfide (disulfide).

Compared structures

  • 1FDL · Crystallographic refinement of the three-dimensional structure of the Fab D1.3-lysozyme… · the same entry in another collection · chain L against L, TM-score 1.00

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