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Streptococcus pneumoniae Mevalonate Kinase in Complex with Diphosphomevalonate

Analyse Streptococcus pneumoniae Mevalonate Kinase in Complex with Diphosphomevalonate in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2OI2
Type: protein
Length: 285 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 2.5
Source: Streptococcus pneumoniae
Molecule: Mevalonate kinase
EC: 2.7.1.36
UniProt: Q8DR51
Ligands: DP6, MG
Pockets: 1 · best druggability 0.79

Structure

x-ray diffraction · resolution 2.5 · 1 distinct chain · 46% helix, 23% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Mevalonate kinase (EC 2.7.1.36)	protein	285	46% helix, 23% strand	Q8DR51

Ligands and binding sites

DP6 · (3R)-3-hydroxy-5-{[(R)-hydroxy(phosphonooxy)phosphoryl]oxy}-3-methylpentanoic acid · ligand · chains A
MG · Magnesium ion · metal · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	409	0.79	0.88	53	MG, DP6

Compared structures

2OI2 · Streptococcus pneumoniae mevalonate kinase in complex with diphosphomevalonate · the same entry in another collection · chain A against A, TM-score 1.00

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt Q8DR51
Elsewhere: RCSB PDB 2OI2 · PDBe 2OI2 · UniProt Q8DR51

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