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Crystal structure of mutator mutt from bartonella henselae

Analyse Crystal structure of mutator mutt from bartonella henselae in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3HHJ
Type
protein
Length
261 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Mutator mutt protein
UniProt
Q6G5F4
Ligands
MG
Pockets
4 · best druggability 0.46

Structure

x-ray diffraction · 2 distinct chains · 24% helix, 36% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AMutator mutt proteinprotein13024% helix, 35% strandQ6G5F4
BMutator mutt proteinprotein13124% helix, 36% strandQ6G5F4

Ligands and binding sites

  • MG · Magnesium ion · metal · 2 copies · chains A, B

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11490.460.7624empty
2850.350.7520empty
3810.320.7323empty
4620.300.7415empty

Interfaces

1 interface between chains.

  • A–B · 674 Ų buried · 4 hydrogen bonds · protein-protein

Compared structures

  • 3HHJ · Crystal structure of mutator mutT from Bartonella henselae · the same entry in another collection · chain A against A, TM-score 1.00

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