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Cryoem structure of vibrio cholerae transposon TN6677 aaa+ ATPase tnsc

Analyse Cryoem structure of vibrio cholerae transposon TN6677 aaa+ ATPase tnsc in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7RZY
Type
protein
Length
2,177 residues
Chains
7
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
TN6677 vibrio cholerae transposon tnsc (vchtnsc)
Ligands
ATP
Pockets
20 · best druggability 0.81

Structure

electron microscopy · 1 distinct chain · 47% helix, 5% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
1, 2, 3, 4, 5, 6, 7TN6677 vibrio cholerae transposon tnsc (vchtnsc)protein31147% helix, 5% strand—

Ligands and binding sites

  • ATP · Adenosine-5'-triphosphate · ligand · 7 copies · chains 1, 2, 7, 3, 4, 5, 6

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
18780.810.8390ATP
28260.810.8393ATP
38300.800.8386ATP
48960.800.8284ATP
58660.790.8288ATP

Interfaces

7 interfaces between chains.

  • 1–2 · 1686 Ų buried · 23 hydrogen bonds · protein-protein
  • 2–3 · 1619 Ų buried · 17 hydrogen bonds · protein-protein
  • 6–7 · 1573 Ų buried · 26 hydrogen bonds · protein-protein
  • 4–5 · 1566 Ų buried · 26 hydrogen bonds · protein-protein
  • 3–4 · 1559 Ų buried · 18 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 20 covalent (covalent ligand).

Compared structures

  • 7RZY · CryoEM structure of Vibrio cholerae transposon Tn6677 AAA+ ATPase TnsC · the same entry in another collection · chain 1 against 1, TM-score 1.00

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