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Three-dimensional structure of N-terminal domain of dnab helicase from helicobacter pylori and its interactions with primase

Analyse Three-dimensional structure of N-terminal domain of dnab helicase from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3GXV
Type
protein
Length
293 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Replicative DNA helicase
EC
3.6.1.-
UniProt
O25916
Pockets
4 · best druggability 0.72

Structure

x-ray diffraction · 4 distinct chains · 72% helix, 0% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AReplicative DNA helicase (EC 3.6.1.-)protein12271% helix, 0% strandO25916
BReplicative DNA helicase (EC 3.6.1.-)protein12369% helix, 0% strandO25916
CReplicative DNA helicase (EC 3.6.1.-)protein2282% helix, 0% strandO25916
DReplicative DNA helicase (EC 3.6.1.-)protein2681% helix, 0% strandO25916

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
16820.720.7951empty
2690.370.7817empty
3520.300.7613empty
4640.300.7413empty

Interfaces

5 interfaces between chains.

  • A–B · 597 Ų buried · 9 hydrogen bonds · protein-protein
  • A–C · 392 Ų buried · 1 hydrogen bond · protein-protein
  • A–D · 376 Ų buried · 0 hydrogen bonds · protein-protein
  • C–D · 143 Ų buried · 0 hydrogen bonds · protein-protein
  • B–D · 96 Ų buried · 0 hydrogen bonds · protein-protein

Compared structures

  • 3GXV · Three-dimensional structure of N-terminal domain of DnaB Helicase from Helicobacter… · the same entry in another collection · chain D against D, TM-score 1.00
  • O25916 · AlphaFold monomer V2.0 prediction for replicative DNA helicase (O25916) · a predicted model of the same protein · chain B against A, TM-score 0.97

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