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Crystal structure of human germline antibody IGHV5-51/IGKV3-11

Analyse Crystal structure of human germline antibody IGHV5-51/IGKV3-11 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5I1J
Type
protein
Length
427 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Fab light chain; Fab heavy chain
Pockets
4 · best druggability 0.58

Structure

x-ray diffraction · 2 distinct chains · 7% helix, 51% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
LFab light chainprotein2146% helix, 50% strand—
HFab heavy chainprotein2139% helix, 52% strand—

Ligands and binding sites

  • GOL · Glycerol · additive · chains L, H

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
13990.580.7544empty
22120.500.7636empty
3890.400.7721empty
4920.340.7422empty

Interfaces

1 interface between chains.

  • L–H · 1701 Ų buried · 16 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 5 disulfide (disulfide).

Compared structures

  • 5I1J · Crystal structure of human germline antibody IGHV5-51/IGKV3-11 · the same entry in another collection · chain L against L, TM-score 1.00

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