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Crystal structure of DH270.6 (unliganded) from the DH270 broadly neutralizing N332-glycan dependent lineage

Analyse Crystal structure of DH270.6 (unliganded) from the DH270 broadly neutralizing… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5TQA
Type
protein
Length
882 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
DH270.6 Fab heavy chain; DH270.6 Fab light chain
Pockets
10 · best druggability 0.72

Structure

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

ChainMoleculeTypeResiduesSecondary structureUniProt
H, ADH270.6 Fab heavy chainprotein2305% helix, 50% strand—
L, BDH270.6 Fab light chainprotein2119% helix, 51% strand—

Pockets

10 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
19630.720.7685empty
25310.600.7449empty
34690.560.7355empty
41970.460.7428empty
51050.420.7722empty

Interfaces

5 interfaces between chains.

  • H–L · 1851 Ų buried · 20 hydrogen bonds · protein-protein
  • B–A · 1812 Ų buried · 21 hydrogen bonds · protein-protein
  • H–A · 644 Ų buried · 8 hydrogen bonds · protein-protein
  • H–B · 106 Ų buried · 0 hydrogen bonds · protein-protein
  • L–A · 92 Ų buried · 2 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 9 disulfide (disulfide).

Compared structures

  • 5TQA · Crystal Structure of DH270.6 (unliganded) from the DH270 Broadly Neutralizing N332-Glycan… · the same entry in another collection · chain H against H, TM-score 1.00

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