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Crystal structure of human translationally controlled tumour associated protein

Analyse Crystal structure of human translationally controlled tumour associated protein in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1YZ1
Type
protein
Length
580 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Translationally controlled tumor protein
UniProt
P13693
Pockets
6 · best druggability 0.66

Structure

x-ray diffraction · 4 distinct chains · 38% helix, 32% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ATranslationally controlled tumor proteinprotein14638% helix, 31% strandP13693
BTranslationally controlled tumor proteinprotein14537% helix, 32% strandP13693
CTranslationally controlled tumor proteinprotein14537% helix, 32% strandP13693
DTranslationally controlled tumor proteinprotein14439% helix, 31% strandP13693

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12250.660.8431empty
21490.620.8527empty
33080.540.7535empty
41120.360.7320empty
5600.300.7414empty

Interfaces

4 interfaces between chains.

  • A–D · 372 Ų buried · 2 hydrogen bonds · protein-protein
  • B–C · 370 Ų buried · 11 hydrogen bonds · protein-protein
  • A–C · 242 Ų buried · 1 hydrogen bond · protein-protein
  • B–D · 131 Ų buried · 1 hydrogen bond · protein-protein

Compared structures

  • 1YZ1 · Crystal structure of human translationally controlled tumour associated protein · the same entry in another collection · chain D against D, TM-score 1.00
  • P13693 · AlphaFold monomer V2.0 prediction for translationally-controlled tumor protein (P13693) · a predicted model of the same protein · chain D against A, TM-score 0.98

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