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Crystal structure of mevalonate diphosphate decarboxylase from staphylococcus aureus (orthorhombic form)

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

PDB: 2HK3
Type: protein
Length: 662 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Diphosphomevalonate decarboxylase
EC: 4.1.1.33
UniProt: Q2FJ52
Pockets: 5 · best druggability 0.76

Structure

x-ray diffraction · 1 distinct chain · 41% helix, 25% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Diphosphomevalonate decarboxylase (EC 4.1.1.33)	protein	331	41% helix, 25% strand	Q2FJ52

Pockets

5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	559	0.76	0.83	56	empty
2	532	0.75	0.82	60	empty
3	155	0.47	0.77	23	empty
4	82	0.37	0.76	16	empty
5	79	0.34	0.75	20	empty

Interfaces

1 interface between chains.

A–B · 1156 Å² buried · 2 hydrogen bonds · protein-protein

Compared structures

2HK3 · Crystal structure of mevalonate diphosphate decarboxylase from Staphylococcus aureus… · 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 Q2FJ52
Elsewhere: RCSB PDB 2HK3 · PDBe 2HK3 · UniProt Q2FJ52

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