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Crystal structure of apo human TUT1, form I

Analyse Crystal structure of apo human TUT1, form I in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5WU1
Type
protein
Length
977 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Speckle targeted PIP5K1A-regulated POLY(A) polymerase
EC
2.7.7.19, 2.7.7.52
UniProt
Q9H6E5
Ligands
CL
Pockets
12 · best druggability 0.69

Structure

x-ray diffraction · 2 distinct chains · 45% helix, 15% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ASpeckle targeted PIP5K1A-regulated POLY(A) polymerase (EC 2.7.7.19, 2.7.7.52)protein49346% helix, 15% strandQ9H6E5
BSpeckle targeted PIP5K1A-regulated POLY(A) polymerase (EC 2.7.7.19, 2.7.7.52)protein48445% helix, 15% strandQ9H6E5

Ligands and binding sites

  • CL · Chloride ion · ion · 2 copies · chains A, B

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
15820.690.7846empty
25240.680.7943empty
32770.580.7842empty
42640.580.7842empty
53570.550.7433empty

Interfaces

1 interface between chains.

  • A–B · 527 Ų buried · 2 hydrogen bonds · protein-protein

Compared structures

  • 5WU1 · Crystal structure of apo human Tut1, form I · the same entry in another collection · chain A against A, TM-score 1.00
  • Q9H6E5 · AlphaFold monomer V2.0 prediction for speckle targeted PIP5K1A-regulated POLY(A)… · a predicted model of the same protein · chain B against A, TM-score 0.99

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