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Structure of farnesyl pyrophosphate synthetase

Analyse Structure of farnesyl pyrophosphate synthetase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1UBW
Type: protein
Length: 348 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Farnesyl diphosphate synthase
EC: 2.5.1.1
UniProt: P08836
Ligands: GPP, MG
Pockets: 3 · best druggability 0.78

Structure

x-ray diffraction · 1 distinct chain · 71% helix, 1% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Farnesyl diphosphate synthase (EC 2.5.1.1)	protein	348	71% helix, 1% strand	P08836

Ligands and binding sites

GPP · Geranyl diphosphate · ligand · chains A
MG · Magnesium ion · metal · 2 copies · chains A

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

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	1100	0.78	0.80	83	MG, GPP
2	121	0.56	0.83	17	empty
3	53	0.27	0.74	14	empty

Compared structures

1UBW · Structure of farnesyl pyrophosphate synthetase · the same entry in another collection · chain A against A, TM-score 1.00
P08836 · AlphaFold monomer V2.0 prediction for farnesyl pyrophosphate synthase (P08836) · a predicted model of the same protein · chain A against A, TM-score 0.96

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 P08836
Elsewhere: RCSB PDB 1UBW · PDBe 1UBW · UniProt P08836

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