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Crystal structure of human germline antibody IGHV3-53/IGKV3-11

Analyse Crystal structure of human germline antibody IGHV3-53/IGKV3-11 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5I1G
Type
protein
Length
424 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Fab light chain; Fab heavy chain
Ligands
SO4
Pockets
1 · best druggability 0.63

Structure

x-ray diffraction · 2 distinct chains · 5% helix, 50% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
LFab light chainprotein2116% helix, 51% strand—
HFab heavy chainprotein2134% helix, 48% strand—

Ligands and binding sites

  • SO4 · Sulfate ion · ion · chains H

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
16300.630.7474empty

Interfaces

1 interface between chains.

  • L–H · 1735 Ų buried · 10 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 4 disulfide (disulfide).

Compared structures

  • 5I1G · Crystal structure of human germline antibody IGHV3-53/IGKV3-11 · the same entry in another collection · chain L against L, TM-score 1.00

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