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Crystal structure of putative CTP pyrophosphohydrolase from bacteroides fragilis

Analyse Crystal structure of putative CTP pyrophosphohydrolase from bacteroides fragilis in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3GWY
Type
protein
Length
254 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Putative CTP pyrophosphohydrolase
UniProt
Q5LBB1
Pockets
3 · best druggability 0.51

Structure

x-ray diffraction · 2 distinct chains · 22% helix, 40% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
APutative CTP pyrophosphohydrolaseprotein12123% helix, 40% strandQ5LBB1
BPutative CTP pyrophosphohydrolaseprotein13321% helix, 41% strandQ5LBB1

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12400.510.7528empty
21610.480.7728empty
31070.400.7617empty

Interfaces

1 interface between chains.

  • A–B · 1006 Ų buried · 14 hydrogen bonds · protein-protein

Compared structures

  • 3GWY · Crystal structure of putative CTP pyrophosphohydrolase from Bacteroides fragilis · the same entry in another collection · chain A against A, TM-score 1.00

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