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Crystal structure of anti-rabies glycoprotein Fab 523-11

Analyse Crystal structure of anti-rabies glycoprotein Fab 523-11 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
4M43
Type
protein
Length
432 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Fragment antigen-binding 523-11 light chain; Fragment antigen-binding 523-11 heavy chain
Ligands
SO4
Pockets
4 · best druggability 0.64

Structure

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

ChainMoleculeTypeResiduesSecondary structureUniProt
LFragment antigen-binding 523-11 light chainprotein2136% helix, 52% strand—
HFragment antigen-binding 523-11 heavy chainprotein2198% helix, 51% strand—

Ligands and binding sites

  • SO4 · Sulfate ion · ion · 3 copies · chains L, H
  • GOL · Glycerol · additive · 2 copies · chains H, L

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
16000.640.7561empty
21730.510.7825empty
3900.380.7615GOL
4520.260.7318empty

Interfaces

1 interface between chains.

  • L–H · 1808 Ų buried · 26 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 4 disulfide (disulfide).

Compared structures

  • 4M43 · Crystal structure of anti-rabies glycoprotein Fab 523-11 · the same entry in another collection · chain L against L, TM-score 1.00

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