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Crystal structure of the ISHP608 transposase in complex with right end 31-mer DNA

Analyse Crystal structure of the ISHP608 transposase in complex with right end 31-mer… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2VHG
Type
protein + DNA
Length
300 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Transposase orfa; Right end 31-mer
UniProt
Q933Z0
Ligands
MN
Pockets
3 · best druggability 0.62

Structure

x-ray diffraction · 4 distinct chains · 38% helix, 28% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ATransposase orfaprotein12638% helix, 29% strandQ933Z0
BTransposase orfaprotein12739% helix, 28% strandQ933Z0
CRight end 31-merdna23——
DRight end 31-merdna24——

Ligands and binding sites

  • MN · Manganese (II) ion · metal · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
14340.620.7752empty
22240.520.7732empty
31700.490.7824empty

Interfaces

5 interfaces between chains.

  • A–B · 1710 Ų buried · 33 hydrogen bonds · protein-protein
  • A–C · 602 Ų buried · 10 hydrogen bonds · protein-nucleic
  • B–D · 601 Ų buried · 13 hydrogen bonds · protein-nucleic
  • A–D · 372 Ų buried · 7 hydrogen bonds · protein-nucleic
  • B–C · 371 Ų buried · 7 hydrogen bonds · protein-nucleic

Compared structures

  • 2VHG · Crystal Structure of the ISHp608 Transposase in Complex with Right End 31-mer DNA · the same entry in another collection · chain A against A, TM-score 1.00

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