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Mub is an aaaplus ATPase that forms helical filaments to control target selection for DNA transposition

Analyse Mub is an aaaplus ATPase that forms helical filaments to control target… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
4BT0
Type
protein
Length
246 residues
Chains
2
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Transcriptional regulator
UniProt
O67198
Ligands
ADP
Pockets
3 · best druggability 0.46

Structure

electron microscopy · 2 distinct chains · 43% helix, 14% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ATranscriptional regulatorprotein7363% helix, 5% strandO67198
BTranscriptional regulatorprotein17335% helix, 17% strandO67198

Ligands and binding sites

  • ADP · Adenosine-5'-diphosphate · ligand · 2 copies · chains A, B

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

Pockets

3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11050.460.7923empty
21320.400.7523empty
3610.360.7813empty

Interfaces

1 interface between chains.

  • A–B · 629 Ų buried · 6 hydrogen bonds · protein-protein

Compared structures

  • 4BT0 · MuB is an AAAplus ATPase that forms helical filaments to control target selection for DNA… · the same entry in another collection · chain A against A, TM-score 1.00

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