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Crystal structure of the anti-pas Fab 3.1 in complex with its epitope peptide

Analyse Crystal structure of the anti-pas Fab 3.1 in complex with its epitope peptide in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7O33
Type
protein
Length
447 residues
Chains
3
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Anti-pas Fab 3.1 chimeric light chain; Anti-pas Fab 3.1 chimeric heavy chain; Apsa…
Pockets
3 · best druggability 0.64

Structure

x-ray diffraction · 3 distinct chains · 7% helix, 50% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
LAnti-pas Fab 3.1 chimeric light chainprotein2195% helix, 51% strand—
HAnti-pas Fab 3.1 chimeric heavy chainprotein2158% helix, 53% strand—
PApsa epitope peptideprotein130% helix, 0% strand—

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
16600.640.7476empty
21980.500.7629empty
3560.310.7614empty

Interfaces

3 interfaces between chains.

  • L–H · 1797 Ų buried · 16 hydrogen bonds · protein-protein
  • H–P · 595 Ų buried · 7 hydrogen bonds · protein-protein
  • L–P · 403 Ų buried · 6 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 5 disulfide, 1 modified (disulfide, cyclization).

Compared structures

  • 7O33 · Crystal structure of the anti-PAS Fab 3.1 in complex with its epitope peptide · the same entry in another collection · chain L against L, TM-score 1.00

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