3m0d

Crystal structure of the TRAF1:TRAF2:cIAP2 complex

Method: X-RAY DIFFRACTION Dmax: 95.3 Å Quality: GOOD

1. Protein Identity and Related Structures Protein Identity & Related Structures

TNF receptor-associated factor 2

Homo sapiens

UniProt Q12933

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 266–329 Chain B; UniProt 266–329 Fragment:Residues 266-329 TNF receptor-associated factor 1 × 1 (Q13077) Baculoviral IAP repeat-containing protein 3 × 1 (Q13489) ZN ZINC ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6;277 K;0.15M AmSO4, 0.1M MES, 15% PEG 4000, pH 6.0, VAPOR DIFFUSION, SITTING DROP, temperature 277K Resolution 2.80 Å R-free 0.247
2 Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 266–329 Chain B; UniProt 266–329 Fragment:Residues 266-329 TNF receptor-associated factor 1 × 1 (Q13077) Baculoviral IAP repeat-containing protein 3 × 1 (Q13489) ZN ZINC ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6;277 K;0.15M AmSO4, 0.1M MES, 15% PEG 4000, pH 6.0, VAPOR DIFFUSION, SITTING DROP, temperature 277K Resolution 2.80 Å R-free 0.247

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

13 other PDB entries and 25 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TRAF2_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–64; UniProt 266–329 Author chain B; PDBConstruct 1–64; UniProt 266–329

TNF receptor-associated factor 1

Homo sapiens

UniProt Q13077

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain C; UniProt 181–244 Fragment:Residues 266-329 TNF receptor-associated factor 2 × 2 (Q12933) Baculoviral IAP repeat-containing protein 3 × 1 (Q13489) ZN ZINC ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6;277 K;0.15M AmSO4, 0.1M MES, 15% PEG 4000, pH 6.0, VAPOR DIFFUSION, SITTING DROP, temperature 277K Resolution 2.80 Å R-free 0.247
2 Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain C; UniProt 181–244 Fragment:Residues 266-329 TNF receptor-associated factor 2 × 2 (Q12933) Baculoviral IAP repeat-containing protein 3 × 1 (Q13489) ZN ZINC ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6;277 K;0.15M AmSO4, 0.1M MES, 15% PEG 4000, pH 6.0, VAPOR DIFFUSION, SITTING DROP, temperature 277K Resolution 2.80 Å R-free 0.247

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

2 other PDB entries and 2 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TRAF1_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain C; PDBConstruct 2–65; UniProt 181–244

Baculoviral IAP repeat-containing protein 3

Homo sapiens

UniProt Q13489

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain D; UniProt 26–99 Fragment:Residues 26-99 TNF receptor-associated factor 2 × 2 (Q12933) TNF receptor-associated factor 1 × 1 (Q13077) ZN ZINC ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6;277 K;0.15M AmSO4, 0.1M MES, 15% PEG 4000, pH 6.0, VAPOR DIFFUSION, SITTING DROP, temperature 277K Resolution 2.80 Å R-free 0.247
2 Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain D; UniProt 26–99 Fragment:Residues 26-99 TNF receptor-associated factor 2 × 2 (Q12933) TNF receptor-associated factor 1 × 1 (Q13077) ZN ZINC ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6;277 K;0.15M AmSO4, 0.1M MES, 15% PEG 4000, pH 6.0, VAPOR DIFFUSION, SITTING DROP, temperature 277K Resolution 2.80 Å R-free 0.247

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

5 other PDB entries and 6 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name BIRC3_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain D; PDBConstruct 2–75; UniProt 26–99

The page prioritizes protein identity, the current assembly, associated components, oligomeric state and cross-PDB links. Chain mapping and sequence ranges are retained as data evidence. Internal IDs, import timestamps and assembly operation expressions are maintenance fields and are not shown here.

SAXS scattering curve SAXS Profile

SAXS profile for 3m0d

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3m0d
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2. Structure Basics 2. Structure Basics

Entry ID entry_id3m0d
Deposition date deposition_date2010-03-02
Structure title titleCrystal structure of the TRAF1:TRAF2:cIAP2 complex
Keywords keywords;trimeric helix coiled coiled, acetylation, alternative splicing, apoptosis, coiled coil, cytoplasm, metal-binding, ubl conjugation, polymorphism, chromosomal rearrangement, SIGNALING PROTEIN ;; SIGNALING PROTEIN
Experimental Method methodX-RAY DIFFRACTION

3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier26.13
Radius of gyration Rg (electron density) rg_electron26.51
Forward intensity I(0) i015618200.00
Molecular weight molecular_weight29359.0 kDa
Excluded volume excluded_volume36522 ų
Envelope volume envelope_volume47212 ų
Hydration-shell volume shell_volume17204 ų
Envelope diameter envelope_diameter97.5
Shell Rg shell_rg29.25
Envelope Rg envelope_rg27.13
Shape Rg shape_rg26.48
Total Rg total_rg26.94
Total atoms total_atoms2047
Residues n_residues264
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 −1
Data points n_points101
Shell type shell_typedirectional
Solvent electron density solvent_density0.3340 e/ų
Shell contrast contrast_shell0.0300 e/ų
CRYSOL version crysol_version4.1.3

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax95.3
Rg (real space) rg_real26.51
Rg uncertainty (real space) rg_real_error1.20
I(0) (real space) i0_real1.5620e+07
I(0) uncertainty (real space) i0_real_error2.6990e+05
Rg (reciprocal space) rg_reciprocal26.39
I(0) (reciprocal space) i0_reciprocal15620000.0000
Solution quality estimate total_estimate0.7811
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary20.3
Skewness Skewness skewness0.622
Kurtosis Kurtosis kurtosis-0.081
Angular range angular_range— – 0.3050 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha2376000.0000
Real-space data points n_real_points62
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.624; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.384; Smooth: 0.894

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 4 domains

CATH v4.4 (4 domains)

Domain ID domain_id3m0dA00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology5 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily170
Domain ID domain_id3m0dB00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology5 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily170
Domain ID domain_id3m0dC00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology5 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily110
Domain ID domain_id3m0dD00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology1170 — Inhibitor Of Apoptosis Protein (2mihbC-IAP-1); Chain A
Homologous superfamily homologous superfamily10 — Inhibitor Of Apoptosis Protein (2mihbC-IAP-1); Chain A

8. Citations (1)

9. Files and Curves (10)