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Crystal structure of T.TH. HB8 CTP synthetase

Analyse Crystal structure of T.TH. HB8 CTP synthetase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1VCM
Type
protein
Length
531 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
CTP synthetase
EC
6.3.4.2
UniProt
Q5SIA8
Pockets
5 · best druggability 0.55

Structure

x-ray diffraction · 1 distinct chain · 39% helix, 21% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ACTP synthetase (EC 6.3.4.2)protein53139% helix, 21% strandQ5SIA8

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12650.550.7743empty
21430.480.7823empty
3810.470.8216empty
4570.330.7714empty
5570.290.7513empty

Compared structures

  • 1VCM · Crystal Structure of T.th. HB8 CTP synthetase · the same entry in another collection · chain A against A, TM-score 1.00
  • Q5SIA8 · AlphaFold monomer V2.0 prediction for CTP synthase (Q5SIA8) · a predicted model of the same protein · chain A against A, TM-score 0.98

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