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Crystal form B1

Analyse Crystal form B1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2R6D
Type
protein
Length
2,340 residues
Chains
6
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Replicative helicase
UniProt
Q9X4C9
Pockets
20 · best druggability 0.77

Structure

x-ray diffraction · 4 distinct chains · 50% helix, 14% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AReplicative helicaseprotein40552% helix, 14% strandQ9X4C9
B, DReplicative helicaseprotein37649% helix, 15% strandQ9X4C9
CReplicative helicaseprotein39950% helix, 13% strandQ9X4C9
E, FReplicative helicaseprotein39248% helix, 14% strandQ9X4C9

Pockets

20 pockets found on a 1 Å grid, 11 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
18110.770.8174empty
27480.760.8173empty
38120.740.7873empty
48610.710.7675empty
57750.700.7776empty

Interfaces

9 interfaces between chains.

  • A–F · 2613 Ų buried · 15 hydrogen bonds · protein-protein
  • B–C · 2503 Ų buried · 17 hydrogen bonds · protein-protein
  • D–E · 1929 Ų buried · 10 hydrogen bonds · protein-protein
  • E–F · 1597 Ų buried · 26 hydrogen bonds · protein-protein
  • A–B · 1575 Ų buried · 18 hydrogen bonds · protein-protein

Compared structures

  • 2R6D · Crystal Form B1 · the same entry in another collection · chain A against A, TM-score 1.00

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