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Crystal structure of geranylgeranyl pyrophosphate synthase from corynebacterium glutamicum complexed with calcium and isoprenyl diphosphate

Analyse Crystal structure of geranylgeranyl pyrophosphate synthase from corynebacterium… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3Q2Q
Type: protein
Length: 314 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Geranylgeranyl pyrophosphate synthase
EC: 2.5.1.30, 2.5.1.-
UniProt: Q8NT37
Ligands: DMA, CA
Pockets: 2 · best druggability 0.64

Structure

x-ray diffraction · 1 distinct chain · 75% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Geranylgeranyl pyrophosphate synthase (EC 2.5.1.30, 2.5.1.-)	protein	314	75% helix, 0% strand	Q8NT37

Ligands and binding sites

DMA · Dimethylallyl diphosphate · ligand · chains A
CA · Calcium ion · metal · 3 copies · chains A
GOL · Glycerol · additive · 2 copies · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	499	0.64	0.76	50	DMA, CA, GOL
2	63	0.33	0.76	16	empty

Compared structures

3Q2Q · Crystal structure of geranylgeranyl pyrophosphate synthase from Corynebacterium… · 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 Q8NT37
Elsewhere: RCSB PDB 3Q2Q · PDBe 3Q2Q · UniProt Q8NT37

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