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Crystal structure of the hydroxyglutarate synthase from pseudomonas putida

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

PDB
6W1G
Type
protein
Length
434 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Hydroxyglutarate synthase
UniProt
Q88CC1
Ligands
NI
Pockets
4 · best druggability 0.73

Structure

x-ray diffraction · 1 distinct chain · 51% helix, 17% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AHydroxyglutarate synthaseprotein43451% helix, 17% strandQ88CC1

Ligands and binding sites

  • NI · Nickel (II) ion · metal · chains A

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
16800.730.7955NI
22630.710.8634empty
3990.360.7522empty
4710.340.7617empty

Compared structures

  • 6W1G · Crystal structure of the hydroxyglutarate synthase from Pseudomonas putida · the same entry in another collection · chain A against A, TM-score 1.00

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