3M06: TRAF2

Crystal Structure of TRAF2. Determined by X-ray diffraction at 2.67 Å resolution. Released 28 Apr 2010.

Method
X-ray diffraction
Resolution
2.67 Å
Organism
Homo sapiens
Chains
6
Atoms
2,686
Mol. weight
50.41 kDa
Released
28 Apr 2010

Explore 3M06 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3M06 contains 9 α-helices and 0 β-strands across 6 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chains A and F: 1 helix, 0 β-strands

ElementResiduesLengthSheet
α-helix268-32659
Chain B: 3 helices, 0 β-strands
ElementResiduesLengthSheet
α-helix268-30639
α-helix313-3164
α-helix318-3247
Chain C: 1 helix, 0 β-strands
ElementResiduesLengthSheet
α-helix268-32760
Chain D: 1 helix, 0 β-strands
ElementResiduesLengthSheet
α-helix268-32457
Chain E: 2 helices, 0 β-strands
ElementResiduesLengthSheet
α-helix268-29528
α-helix299-32527

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
TNF receptor-associated factor 2A, B, C, D, E, Fprotein72Homo sapiensQ12933 (AlphaFold model)
Sequence of entity 1 (A, B, C, D, E, F), FASTA
>3M06_1 TNF receptor-associated factor 2 (chains A, B, C, D, E, F)
SELLQRCESLEKKTATFENIVCVLNREVERVAMTAEACSRQHRLDQDKIEALSSKVQQLE
RSIGLEHHHHHH

Primary citation

Crystal structures of the TRAF2: cIAP2 and the TRAF1: TRAF2: cIAP2 complexes: affinity, specificity, and regulation. Zheng, C., Kabaleeswaran, V., Wang, Y. et al. Mol Cell (2010) 38:101-113. DOI 10.1016/j.molcel.2010.03.009 · PubMed

Other PDB entries of the same protein (UniProt Q12933 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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