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Crystal structure of a putative farnesyl-diphosphate synthase from Marinomonas sp. MED121 (Target EFI-501980)

Analyse Crystal structure of a putative farnesyl-diphosphate synthase from Marinomonas… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
4F62
Type
protein
Length
522 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v2 / PDB Bank
Contract
0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner
0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution
2.101
Source
Marinomonas sp. MED121
Molecule
Geranyltranstransferase
EC
2.5.1.-
UniProt
A3YCB7
Ligands
SO4, CL
Pockets
4 · best druggability 0.61

Structure

x-ray diffraction · resolution 2.101 · 2 distinct chains · 79% helix, 0% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AGeranyltranstransferase (EC 2.5.1.-)protein26779% helix, 0% strandA3YCB7
BGeranyltranstransferase (EC 2.5.1.-)protein25579% helix, 0% strandA3YCB7

Ligands and binding sites

  • SO4 · Sulfate ion · ion · chains A
  • CL · Chloride ion · ion · chains A, B
  • GOL · Glycerol · additive · 2 copies · chains A, B

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
13180.610.7850GOL
22780.540.7539GOL
3760.390.7819empty
4730.340.7522GOL

Interfaces

1 interface between chains.

  • A–B · 2179 Ų buried · 27 hydrogen bonds · protein-protein

Compared structures

  • 4F62 · Crystal structure of a putative farnesyl-diphosphate synthase from marinomonas sp. MED121… · the same entry in another collection · chain A against A, TM-score 1.00

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