1CZY: PDB entry 1CZY

Crystal structure of the complex between the traf domain of human TRAF2 and an LMP1 binding peptide. Determined by X-ray diffraction at 2.0 Å resolution. Released 8 Mar 2000.

Method: X-ray diffraction
Resolution: 2.0 Å
Organism: Homo sapiens
Chains: 5
Atoms: 4,348
Mol. weight: 58.7 kDa
Released: 8 Mar 2000

Explore 1CZY in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1CZY contains 27 α-helices and 35 β-strands across 5 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: 9 helices, 10 β-strands

Element	Residues	Length	Sheet
α-helix	335-347	13
β-strand	353-358	6	1
α-helix	361-369	9
β-strand	376-377	2	2
α-helix	378-380	3
β-strand	381-382	2	2
β-strand	389-395	7	2
α-helix	400-402	3
β-strand	406-414	9	2
α-helix	419-421	3
β-strand	430-434	5	1
β-strand	443-447	5	1
α-helix	454-456	3
α-helix	458-459	2
β-strand	463	1	2
α-helix	464-466	3
β-strand	467-474	8	2
α-helix	476-480	5
β-strand	490-496	7	1

Chain B: 9 helices, 11 β-strands

Element	Residues	Length	Sheet
α-helix	335-347	13
β-strand	353-359	7	3
α-helix	361-369	9
β-strand	376-377	2	4
α-helix	378-380	3
β-strand	381-382	2	4
β-strand	389-395	7	4
α-helix	400-402	3
β-strand	406-414	9	4
α-helix	419-421	3
β-strand	430-434	5	3
β-strand	443-447	5	3
α-helix	454-456	3
α-helix	458-459	2
β-strand	463	1	4
α-helix	464-466	3
β-strand	467-474	8	4
α-helix	476-480	5
β-strand	486	1	3
β-strand	489-496	8	3

Chain C: 9 helices, 12 β-strands

Element	Residues	Length	Sheet
α-helix	335-347	13
β-strand	353-358	6	5
α-helix	361-369	9
β-strand	376-377	2	6
α-helix	378-380	3
β-strand	381-382	2	6
β-strand	389-395	7	6
α-helix	400-402	3
β-strand	406-414	9	6
α-helix	419-421	3
β-strand	430-434	5	5
β-strand	443-447	5	5
α-helix	454-456	3
α-helix	458-459	2
β-strand	463	1	6
α-helix	464-466	3
β-strand	467-474	8	6
α-helix	476-480	5
β-strand	486	1	7
β-strand	489	1	7
β-strand	490-496	7	5

Chains D and E: 0 helices, 1 β-strand

Element	Residues	Length	Sheet
β-strand	205-206	2	2

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Tumor necrosis factor receptor associated protein 2	A, B, C	protein	168	Homo sapiens	Q12933 (AlphaFold model)
Latent membrane protein 1	D, E	protein	8		P03230 (AlphaFold model)

Sequence of entity 1 (A, B, C), FASTA

>1CZY_1 TUMOR NECROSIS FACTOR RECEPTOR ASSOCIATED PROTEIN 2 (chains A, B, C)
AMADLEQKVLEMEASTYDGVFIWKISDFPRKRQEAVAGRIPAIFSPAFYTSRYGYKMCLR
IYLNGDGTGRGTHLSLFFVVMKGPNDALLRWPFNQKVTLMLLDQNNREHVIDAFRPDVTS
SSFQRPVNDMNIASGCPLFCPVSKMEAKNSYVRDDAIFIKAIVDLTGL

Sequence of entity 2 (D, E), FASTA

>1CZY_2 LATENT MEMBRANE PROTEIN 1 (chains D, E)
XPQQATDD

Primary citation

The structural basis for the recognition of diverse receptor sequences by TRAF2. Ye, H., Park, Y.C., Kreishman, M. et al. Mol Cell (1999) 4:321-330. DOI 10.1016/S1097-2765(00)80334-2 · 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
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
3M06 2.67 Å, Crystal Structure of TRAF2

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