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Crystal structure of bacillus stearothermophilus farnesyl pyrophosphate synthase

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

PDB
5AYP
Type
protein
Length
522 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Farnesyl diphosphate synthase
EC
2.5.1.10
UniProt
Q08291
Pockets
5 · best druggability 0.60

Structure

x-ray diffraction · 2 distinct chains · 76% helix, 1% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AFarnesyl diphosphate synthase (EC 2.5.1.10)protein25875% helix, 2% strandQ08291
BFarnesyl diphosphate synthase (EC 2.5.1.10)protein26477% helix, 0% strandQ08291

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
13630.600.7743empty
23240.590.7842empty
3940.380.7610empty
41020.380.7510empty
5710.360.7613empty

Interfaces

1 interface between chains.

  • A–B · 2048 Ų buried · 7 hydrogen bonds · protein-protein

Compared structures

  • 5AYP · Crystal structure of Bacillus stearothermophilus Farnesyl pyrophosphate synthase · the same entry in another collection · chain A against A, TM-score 1.00
  • Q08291 · AlphaFold monomer V2.0 prediction for farnesyl diphosphate synthase (Q08291) · a predicted model of the same protein · chain B against A, TM-score 0.98

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