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Orthorhombic form of human IGA1 Fab fragment, sharing same fv as IgG

Analyse Orthorhombic form of human IGA1 Fab fragment, sharing same fv as IgG in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3QNX
Type
protein
Length
438 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Fab fragment of immunoglobulin A1 light chain; Fab fragment of immunoglobulin A1 heavy…
Pockets
3 · best druggability 0.64

Structure

x-ray diffraction · 2 distinct chains · 5% helix, 51% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AFab fragment of immunoglobulin A1 light chainprotein2195% helix, 50% strand—
BFab fragment of immunoglobulin A1 heavy chainprotein2194% helix, 51% strand—

Ligands and binding sites

  • GOL · Glycerol · additive · 3 copies · chains A, B

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
15610.640.7670empty
21080.360.7324GOL
3650.290.7318empty

Interfaces

1 interface between chains.

  • A–B · 1662 Ų buried · 25 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 6 disulfide (disulfide).

Compared structures

  • 3QNX · Orthorhombic form of human IgA1 Fab fragment, sharing same Fv as IgG · the same entry in another collection · chain A against A, TM-score 1.00

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