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Crystal structure of the anti-human P-cadherin Fab CQY684

Analyse Crystal structure of the anti-human P-cadherin Fab CQY684 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6ZTF
Type
protein
Length
879 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
CQY684 Fab heavy-chain; CQY684 Fab light-chain
Pockets
9 · best druggability 0.63

Structure

x-ray diffraction · 4 distinct chains · 7% helix, 52% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ACQY684 Fab heavy-chainprotein2339% helix, 50% strand—
BCQY684 Fab light-chainprotein2116% helix, 52% strand—
HCQY684 Fab heavy-chainprotein2256% helix, 53% strand—
LCQY684 Fab light-chainprotein2106% helix, 52% strand—

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
16430.630.7464empty
25680.600.7365empty
32290.470.7341empty
4640.460.8323empty
51200.390.7522empty

Interfaces

3 interfaces between chains.

  • H–L · 1808 Ų buried · 18 hydrogen bonds · protein-protein
  • A–B · 1707 Ų buried · 16 hydrogen bonds · protein-protein
  • B–L · 322 Ų buried · 4 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 8 disulfide (disulfide).

Compared structures

  • 6ZTF · Crystal Structure of the anti-human P-Cadherin Fab CQY684 · the same entry in another collection · chain A against A, TM-score 1.00

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