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Human mabs broadly protect against infection of arthritiogenic alphaviruses by recognizing conserved elements of the MXR8 receptor binding domain

Analyse Human mabs broadly protect against infection of arthritiogenic alphaviruses by… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6W1C
Type
protein
Length
4,596 residues
Chains
16
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
E1 glycoprotein; E2 glycoprotein; Fab chk-265 heavy chain; Fab chk-265 light chain
UniProt
Q8QZ72
Pockets
20 · best druggability 0.75

Structure

electron microscopy · 4 distinct chains · 3% helix, 35% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, C, DE1 glycoproteinprotein3803% helix, 33% strandQ8QZ72
E, F, G, HE2 glycoproteinprotein3403% helix, 32% strandQ8QZ72
I, J, K, LFab chk-265 heavy chainprotein2181% helix, 45% strand—
M, N, O, PFab chk-265 light chainprotein2115% helix, 36% strand—

Pockets

20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
111510.750.79178empty
210490.750.78166empty
35540.750.8393empty
48430.740.7993empty
511130.740.78122empty

Interfaces

21 interfaces between chains.

  • I–M · 604 Ų buried · 12 hydrogen bonds · protein-protein
  • L–P · 563 Ų buried · 7 hydrogen bonds · protein-protein
  • K–O · 541 Ų buried · 6 hydrogen bonds · protein-protein
  • C–G · 534 Ų buried · 14 hydrogen bonds · protein-protein
  • A–E · 530 Ų buried · 17 hydrogen bonds · protein-protein

Compared structures

  • 6W1C · Human mAbs broadly protect against infection of arthritiogenic alphaviruses by… · the same entry in another collection · chain A against A, TM-score 1.00

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