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Crystal structure of citrate synthase from thermus thermophilus HB8

Analyse Crystal structure of citrate synthase from thermus thermophilus HB8 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1IOM
Type
protein
Length
374 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Citrate synthase
EC
4.1.3.7
UniProt
Q9LCX9
Ligands
SO4, CO3
Pockets
1 · best druggability 0.55

Structure

x-ray diffraction · 1 distinct chain · 60% helix, 3% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ACitrate synthase (EC 4.1.3.7)protein37460% helix, 3% strandQ9LCX9

Ligands and binding sites

  • SO4 · Sulfate ion · ion · chains A
  • CO3 · Carbonate ion · ion · chains A
  • GOL · Glycerol · additive · 3 copies · chains A

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

Pockets

1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12820.550.7645CO3, GOL

Compared structures

  • 1IOM · Crystal structure of citrate synthase from thermus thermophilus HB8 · the same entry in another collection · chain A against A, TM-score 1.00

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