3HCU: TRAF6

Crystal structure of TRAF6 in complex with Ubc13 in the C2 space group. Determined by X-ray diffraction at 2.6 Å resolution. Released 26 May 2009.

Method: X-ray diffraction
Resolution: 2.6 Å
Organism: Homo sapiens
Chains: 4
Atoms: 4,098
Mol. weight: 62.82 kDa
Ligands: ZN
Released: 26 May 2009

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

Secondary structure: helices and β-sheets

3HCU contains 27 α-helices and 36 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: 6 helices, 11 β-strands

Element	Residues	Length	Sheet
β-strand	56	1	1
β-strand	60	1	2
α-helix	63-65	3
α-helix	66-68	3
β-strand	69	1	1
β-strand	76	1	1
β-strand	80-82	3	3
β-strand	88-90	3	3
α-helix	91-99	9
β-strand	104	1	4
β-strand	111	1	4
α-helix	114-116	3
β-strand	118-119	2	3
α-helix	121-127	7
β-strand	131-133	3	2
β-strand	142-144	3	2
α-helix	145-152	8

Chains B and D: 8 helices, 7 β-strands

Element	Residues	Length	Sheet
α-helix	6-17	12
α-helix	19-20	2
β-strand	23-28	6	5
β-strand	31-40	10	5
α-helix	41-42	2
β-strand	51-57	7	5
α-helix	66-67	2
β-strand	68-71	4	5
β-strand	80	1	6
β-strand	85	1	5
β-strand	86	1	6
α-helix	89-91	3
α-helix	101-113	13
α-helix	123-131	9
α-helix	133-147	15

Chain C: 5 helices, 11 β-strands

Element	Residues	Length	Sheet
β-strand	56	1	7
β-strand	60	1	8
β-strand	69	1	7
β-strand	76	1	7
β-strand	81-82	2	9
β-strand	88-89	2	9
α-helix	91-96	6
α-helix	97-101	5
β-strand	104	1	10
β-strand	111	1	10
α-helix	121-127	7
β-strand	131	1	11
β-strand	132	1	8
β-strand	144	1	11
α-helix	145-147	3
α-helix	150-153	4

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
TNF receptor-associated factor 6	A, C	protein	118	Homo sapiens	Q9Y4K3 (AlphaFold model)
Ubiquitin-conjugating enzyme E2 N	B, D	protein	155	Homo sapiens	P61088 (AlphaFold model)

Sequence of entity 1 (A, C), FASTA

>3HCU_1 TNF receptor-associated factor 6 (chains A, C)
MEEIQGYDVEFDPPLESKYECPICLMALREAVQTPCGHRFCKACIIKSIRDAGHKCPVDN
EILLENQLFPDNFAKREILSLMVKCPNEGCLHKMELRHLEDHQAHCEFALLEHHHHHH

Sequence of entity 2 (B, D), FASTA

>3HCU_2 Ubiquitin-conjugating enzyme E2 N (chains B, D)
GSHMAGLPRRIIKETQRLLAEPVPGIKAEPDESNARYFHVVIAGPQDSPFEGGTFKLELF
LPEEYPMAAPKVRFMTKIYHPNVDKLGRICLDILKDKWSPALQIRTVLLSIQALLSAPNP
DDPLANDVAEQWKTNEAQAIETARAWTRLYAMNNI

Ligands and cofactors

ID	Name	Formula	Copies
ZN	Zinc ion	Zn	6

Primary citation

E2 interaction and dimerization in the crystal structure of TRAF6. Yin, Q., Lin, S.C., Lamothe, B. et al. Nat Struct Mol Biol (2009) 16:658-666. DOI 10.1038/nsmb.1605 · PubMed

Other PDB entries of the same protein (UniProt Q9Y4K3 (AlphaFold model), which also has an AlphaFold model), best resolution first:

1LB6 1.8 Å, TRAF6-CD40 Complex
3HCT 2.1 Å, Crystal structure of TRAF6 in complex with Ubc13 in the P1 space group
6A33 2.1 Å, Binding and Enhanced Binding between Key Immunity Proteins TRAF6 and TIFA
3HCS 2.2 Å, Crystal structure of the N-terminal domain of TRAF6
1LB4 2.4 Å, TRAF6 apo structure
1LB5 2.4 Å, TRAF6-RANK Complex
5ZUJ 2.6 Å, Binding and Enhanced Binding between Key Immunity Proteins TRAF6 and TIFA
8HZ2 2.6 Å, Tumor Necrosis Factor Receptor Associated Factor 6 (TRAF6) N-terminal Domain
7L3L 2.8 Å, Structure of TRAF5 and TRAF6 RING Hetero dimer
4Z8M 2.95 Å, Crystal structure of the MAVS-TRAF6 complex
2ECI Solution structure of the RING domain of the human TNF receptor-associated factor 6…
2JMD Solution Structure of the Ring Domain of Human TRAF6

Browse structure collections

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