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Crystal structure of human translationally controlled tumour associated protein (htctp) mutant E12V

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
3EBM
Type
protein
Length
583 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 0.70

Structure

x-ray diffraction · 4 distinct chains · 36% helix, 32% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ATranslationally-controlled tumor proteinprotein14737% helix, 31% strandP13693
BTranslationally-controlled tumor proteinprotein14736% helix, 32% strandP13693
CTranslationally-controlled tumor proteinprotein14539% helix, 33% strandP13693
DTranslationally-controlled tumor proteinprotein14433% helix, 32% strandP13693

Pockets

6 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11420.700.9024empty
24000.670.8033empty
32440.630.8129empty
41400.560.8219empty
5890.350.7520empty

Interfaces

3 interfaces between chains.

  • B–C · 702 Ų buried · 12 hydrogen bonds · protein-protein
  • C–D · 383 Ų buried · 5 hydrogen bonds · protein-protein
  • A–B · 287 Ų buried · 6 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

  • 3EBM · Crystal structure of human translationally controlled tumour associated protein (hTCTP)… · 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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