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Crystal structure of HN33/TUSC3-peptide 1

Analyse Crystal structure of HN33/TUSC3-peptide 1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
4M91
Type
protein
Length
159 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Tumor suppressor candidate 3; Protein cereblon
UniProt
Q13454, Q96SW2

Structure

x-ray diffraction · 2 distinct chains · 47% helix, 14% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ATumor suppressor candidate 3protein15349% helix, 14% strandQ13454
BProtein cereblonprotein60% helix, 0% strandQ96SW2

Interfaces

1 interface between chains.

  • A–B · 368 Ų buried · 7 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

  • 4M91 · crystal structure of hN33/Tusc3-peptide 1 · the same entry in another collection · chain A against A, TM-score 1.00
  • Q13454 · AlphaFold monomer V2.0 prediction for tumor suppressor candidate 3 (Q13454) · a predicted model of the same protein · chain A against A, TM-score 0.98
  • Q96SW2 · AlphaFold monomer V2.0 prediction for protein cereblon (Q96SW2) · a predicted model of the same protein · chain B against A, TM-score 0.70

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