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Crystal form BH2

Analyse Crystal form BH2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2R6C
Type
protein
Length
2,562 residues
Chains
9
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Replicative helicase; Dnag primase, helicase binding domain
EC
2.7.7.-
UniProt
Q9X4C9, Q9X4D0
Pockets
20 · best druggability 0.67

Structure

x-ray diffraction · 2 distinct chains · 54% helix, 8% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, C, D, E, FReplicative helicaseprotein35848% helix, 11% strandQ9X4C9
G, H, IDnag primase, helicase binding domain (EC 2.7.7.-)protein13870% helix, 0% strandQ9X4D0

Pockets

20 pockets found on a 1 Å grid, 17 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
15980.670.7759empty
25130.670.7861empty
35970.670.7765empty
45140.650.7752empty
51670.640.8521empty

Interfaces

15 interfaces between chains.

  • C–F · 1434 Ų buried · 5 hydrogen bonds · protein-protein
  • A–D · 1420 Ų buried · 4 hydrogen bonds · protein-protein
  • B–E · 1413 Ų buried · 4 hydrogen bonds · protein-protein
  • E–F · 946 Ų buried · 18 hydrogen bonds · protein-protein
  • C–D · 813 Ų buried · 15 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 18 modified (engineered).

Compared structures

  • 2R6C · Crystal Form BH2 · the same entry in another collection · chain I against I, TM-score 1.00
  • Q9X4D0 · AlphaFold monomer V2.0 prediction for DNA primase (Q9X4D0) · a predicted model of the same protein · chain H against A, TM-score 0.92

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