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Three dimensional structure of an fv from a human IgM immunoglobulin

Analyse Three dimensional structure of an fv from a human IgM immunoglobulin in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1IGM
Type
protein
Length
244 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
IgM-kappa pot fv (light chain); IgM-kappa pot fv (heavy chain)
Pockets
2 · best druggability 0.33

Structure

x-ray diffraction · 2 distinct chains · 4% helix, 44% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
LIgM-kappa pot fv (light chain)protein1153% helix, 45% strand—
HIgM-kappa pot fv (heavy chain)protein1295% helix, 43% strand—

Pockets

2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1880.330.7418empty
2640.290.7320empty

Interfaces

1 interface between chains.

  • L–H · 796 Ų buried · 10 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 disulfide (disulfide).

Compared structures

  • 1IGM · Three dimensional structure of an fv from a human IgM immunoglobulin · the same entry in another collection · chain L against L, TM-score 1.00

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