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Crystal structure of certolizumab Fab

Analyse Crystal structure of certolizumab Fab in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5WUV
Type
protein
Length
433 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Light chain; Heavy chain
Pockets
3 · best druggability 0.60

Structure

x-ray diffraction · 2 distinct chains · 7% helix, 51% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
LLight chainprotein2136% helix, 52% strand—
HHeavy chainprotein2208% helix, 50% strand—

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
15810.600.7356empty
22610.560.7737empty
3670.290.7317empty

Interfaces

1 interface between chains.

  • L–H · 1781 Ų buried · 14 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 4 disulfide (disulfide).

Compared structures

  • 5WUV · Crystal structure of Certolizumab Fab · the same entry in another collection · chain L against L, TM-score 1.00

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