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Crystal structure of anti-alphaVbeta3 integrin Fab LM609

Analyse Crystal structure of anti-alphaVbeta3 integrin Fab LM609 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5OPY
Type
protein
Length
426 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v2 / PDB Bank
Contract
0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner
0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution
2.26
Source
Mus musculus
Molecule
Heavy chain of LM609 Fab (antigen-binding fragment); Light chain of LM609 Fab…
Pockets
4 · best druggability 0.67

Structure

x-ray diffraction · resolution 2.26 · 2 distinct chains · 7% helix, 52% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
HHeavy chain of LM609 Fab (antigen-binding fragment)protein2148% helix, 53% strand—
LLight chain of LM609 Fab (antigen-binding fragment)protein2126% helix, 51% strand—

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
16440.670.7654empty
2920.340.7419empty
3560.330.7714empty
4650.300.7416empty

Interfaces

1 interface between chains.

  • H–L · 1840 Ų buried · 20 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 4 disulfide (disulfide).

Compared structures

  • 5OPY · Crystal structure of anti-ALPHAVBETA3 integrin Fab LM609 · the same entry in another collection · chain H against H, TM-score 1.00

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