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Structure of the pyrococcus furiosus esterase PF2001 with space group P3121

Analyse Structure of the pyrococcus furiosus esterase PF2001 with space group P3121 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5G59
Type
protein
Length
274 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Esterase
UniProt
Q8TZJ1
Ligands
HG
Pockets
2 · best druggability 0.81

Structure

x-ray diffraction · 1 distinct chain · 43% helix, 18% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AEsteraseprotein27443% helix, 18% strandQ8TZJ1

Ligands and binding sites

  • HG · Mercury (II) ion · metal · 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.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
13490.810.9040empty
2940.400.7721empty

Compared structures

  • 5G59 · Structure of the Pyrococcus Furiosus Esterase Pf2001 with space group P3121 · the same entry in another collection · chain A against A, TM-score 1.00

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