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Crystal structure of staphylococcus epidermidis mevalonate diphosphate decarboxylase

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

PDB: 3QT5
Type: protein
Length: 649 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Mevalonate diphosphate decarboxylase
EC: 4.1.1.33
UniProt: Q9FD73
Pockets: 3 · best druggability 0.75

Structure

x-ray diffraction · 2 distinct chains · 42% helix, 26% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Mevalonate diphosphate decarboxylase (EC 4.1.1.33)	protein	327	43% helix, 26% strand	Q9FD73
B	Mevalonate diphosphate decarboxylase (EC 4.1.1.33)	protein	322	41% helix, 26% strand	Q9FD73

Pockets

3 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	480	0.75	0.83	54	empty
2	430	0.68	0.80	58	empty
3	184	0.45	0.74	33	empty

Interfaces

1 interface between chains.

A–B · 1007 Å² buried · 6 hydrogen bonds · protein-protein

Compared structures

3QT5 · Crystal structure of Staphylococcus epidermidis mevalonate diphosphate decarboxylase · 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 Q9FD73
Elsewhere: RCSB PDB 3QT5 · PDBe 3QT5 · UniProt Q9FD73

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