3M0D: TRAF1:TRAF2:cIAP2 complex

Crystal structure of the TRAF1:TRAF2:cIAP2 complex. Determined by X-ray diffraction at 2.8 Å resolution. Released 28 Apr 2010.

Method: X-ray diffraction
Resolution: 2.8 Å
Organism: Homo sapiens
Chains: 4
Atoms: 2,089
Mol. weight: 31.26 kDa
Ligands: ZN
Released: 28 Apr 2010

Explore 3M0D in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3M0D contains 10 α-helices and 3 β-strands across 4 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.

Chain A: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	268-328	61

Chain B: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	268-327	60

Chain C: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	268-326	59

Chain D: 7 helices, 3 β-strands

Element	Residues	Length	Sheet
α-helix	28-33	6
α-helix	34-36	3
α-helix	39-40	2
α-helix	47-52	6
β-strand	55-57	3	1
β-strand	64-66	3	1
β-strand	72-73	2	1
α-helix	76-77	2
α-helix	82-89	8
α-helix	94-98	5

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
TNF receptor-associated factor 2	A, B	protein	66	Homo sapiens	Q12933 (AlphaFold model)
TNF receptor-associated factor 1	C	protein	65	Homo sapiens	Q13077 (AlphaFold model)
Baculoviral IAP repeat-containing protein 3	D	protein	75	Homo sapiens	Q13489 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>3M0D_1 TNF receptor-associated factor 2 (chains A, B)
SELLQRCESLEKKTATFENIVCVLNREVERVAMTAEACSRQHRLDQDKIEALSSKVQQLE
RSIGLE

Sequence of entity 2 (C), FASTA

>3M0D_2 TNF receptor-associated factor 1 (chains C)
MFMKEKLLAELEGKLRVFENIVAVLNKEVEASHLALATSIHQSQLDRERILSLEQRVVEL
QQTLA

Sequence of entity 3 (D), FASTA

>3M0D_3 Baculoviral IAP repeat-containing protein 3 (chains D)
MLSCELYRMSTYSTFPAGVPVSERSLARAGFYYTGVNDKVKCFCCGLMLDNWKRGDSPTE
KHKKLYPSCRFVQSL

Ligands and cofactors

ID	Name	Formula	Copies
ZN	Zinc ion	Zn	1

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:

3KNV 1.9 Å, Crystal structure of the RING and first zinc finger domains of TRAF2
8T5Q 1.9 Å, SARS-CoV-2 ORF3a peptide in complex with TRAF2 TRAF domain
1CZY 2.0 Å, Crystal structure of the complex between the traf domain of human TRAF2 and an LMP1…
1D00 2.0 Å, Structure of tnf receptor associated factor 2 in complex with a 5-residue CD40 peptide
1D01 2.0 Å, Structure of tnf receptor associated factor 2 in complex with a human CD30 peptide
1D0A 2.0 Å, Structure of tnf receptor associated factor 2 (TRAF2) in complex with a human OX40 peptide
1F3V 2.0 Å, Crystal structure of the complex between the N-terminal domain of TRADD and the TRAF…
1CA4 2.2 Å, Structure of tnf receptor associated factor 2 (TRAF2)
1CA9 2.3 Å, Structure of tnf receptor associated factor 2 in complex with a peptide from tnf-R2
1QSC 2.4 Å, Crystal structure of the traf domain of TRAF2 in a complex with a peptide from the CD40…
1D0J 2.5 Å, Structure of tnf receptor associated factor 2 in complex with a M4-1BB peptide
3M0A 2.61 Å, Crystal structure of TRAF2:cIAP2 complex

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