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Crystal structure of the ring and first zinc finger domains of TRAF2

Analyse Crystal structure of the ring and first zinc finger domains of TRAF2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3KNV
Type
protein
Length
123 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
TNF receptor-associated factor 2
UniProt
Q12933
Ligands
ZN

Structure

x-ray diffraction · 1 distinct chain · 38% helix, 17% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ATNF receptor-associated factor 2protein12338% helix, 17% strandQ12933

Ligands and binding sites

  • ZN · Zinc ion · metal · 3 copies · chains A

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

Compared structures

  • 3KNV · Crystal structure of the RING and first zinc finger domains of TRAF2 · the same entry in another collection · chain A against A, TM-score 1.00
  • Q12933 · AlphaFold monomer V2.0 prediction for TNF receptor-associated factor 2 (Q12933) · a predicted model of the same protein · chain A against A, TM-score 0.94

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