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Crystal structure of mevalonate kinase from methicillin- resistant staphylococcus aureus MRSA252

Analyse Crystal structure of mevalonate kinase from methicillin- resistant… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2X7I
Type
protein
Length
295 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Mevalonate kinase
UniProt
Q6GJ78
Ligands
CL
Pockets
4 · best druggability 0.67

Structure

x-ray diffraction · 1 distinct chain · 39% helix, 26% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AMevalonate kinaseprotein29539% helix, 26% strandQ6GJ78

Ligands and binding sites

  • CL · Chloride ion · ion · chains A
  • CIT · Citric acid · additive · chains A

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11060.670.9015empty
21450.600.8525CIT
3750.530.8520empty
4520.360.7916empty

Compared structures

  • 2X7I · Crystal structure of mevalonate kinase from methicillin-resistant Staphylococcus aureus… · the same entry in another collection · chain A against A, TM-score 1.00

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