1d0a

STRUCTURE OF TNF RECEPTOR ASSOCIATED FACTOR 2 (TRAF2) IN COMPLEX WITH A HUMAN OX40 PEPTIDE

Method: X-RAY DIFFRACTION Dmax: 129.6 Å Quality: GOOD

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

TUMOR NECROSIS FACTOR RECEPTOR ASSOCIATED PROTEIN 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 × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain A; UniProt 334–501 Chain B; UniProt 334–501 Chain C; UniProt 334–501 Fragment:TRAF DOMAIN OX40L RECEPTOR PEPTIDE × 3 (P43489) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;pH 6;293 K;PEG4K, MES, PH 6.0, VAPOR DIFFUSION, temperature 293K Resolution 2.00 Å R-free 0.251
2 Protein heterocomplex Heteromer Protein × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain D; UniProt 334–501 Chain E; UniProt 334–501 Chain F; UniProt 334–501 Fragment:TRAF DOMAIN OX40L RECEPTOR PEPTIDE × 3 (P43489) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;pH 6;293 K;PEG4K, MES, PH 6.0, VAPOR DIFFUSION, temperature 293K Resolution 2.00 Å R-free 0.251
3 Protein heterocomplex Heteromer Protein × 12 PDB declaration: dodecameric(12) Consistent with protein copy count Chain A; UniProt 334–501 Chain B; UniProt 334–501 Chain C; UniProt 334–501 Chain D; UniProt 334–501 Chain E; UniProt 334–501 Chain F; UniProt 334–501 Fragment:TRAF DOMAIN OX40L RECEPTOR PEPTIDE × 6 (P43489) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;pH 6;293 K;PEG4K, MES, PH 6.0, VAPOR DIFFUSION, temperature 293K Resolution 2.00 Å R-free 0.251
4 Protein heterocomplex Heteromer Protein × 12 PDB declaration: dodecameric(12) Consistent with protein copy count Chain A; UniProt 334–501 Chain B; UniProt 334–501 Chain C; UniProt 334–501 Chain D; UniProt 334–501 Chain E; UniProt 334–501 Chain F; UniProt 334–501 Fragment:TRAF DOMAIN OX40L RECEPTOR PEPTIDE × 6 (P43489) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;pH 6;293 K;PEG4K, MES, PH 6.0, VAPOR DIFFUSION, temperature 293K Resolution 2.00 Å R-free 0.251

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 23 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 1–168; UniProt 334–501 Author chain B; PDBConstruct 1–168; UniProt 334–501 Author chain C; PDBConstruct 1–168; UniProt 334–501 Author chain D; PDBConstruct 1–168; UniProt 334–501 Author chain E; PDBConstruct 1–168; UniProt 334–501 Author chain F; PDBConstruct 1–168; UniProt 334–501

OX40L RECEPTOR PEPTIDE

OrganismNot specified

UniProt P43489

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 × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain G; UniProt 262–266 Chain H; UniProt 262–266 Chain I; UniProt 262–266 Fragment:TRAF-BINDING SEQUENCE Non-standard monomer:Yes (specific site not provided by mmCIF) TUMOR NECROSIS FACTOR RECEPTOR ASSOCIATED PROTEIN 2 × 3 (Q12933) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;pH 6;293 K;PEG4K, MES, PH 6.0, VAPOR DIFFUSION, temperature 293K Resolution 2.00 Å R-free 0.251
2 Protein heterocomplex Heteromer Protein × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain J; UniProt 262–266 Chain K; UniProt 262–266 Chain L; UniProt 262–266 Fragment:TRAF-BINDING SEQUENCE Non-standard monomer:Yes (specific site not provided by mmCIF) TUMOR NECROSIS FACTOR RECEPTOR ASSOCIATED PROTEIN 2 × 3 (Q12933) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;pH 6;293 K;PEG4K, MES, PH 6.0, VAPOR DIFFUSION, temperature 293K Resolution 2.00 Å R-free 0.251
3 Protein heterocomplex Heteromer Protein × 12 PDB declaration: dodecameric(12) Consistent with protein copy count Chain G; UniProt 262–266 Chain H; UniProt 262–266 Chain I; UniProt 262–266 Chain J; UniProt 262–266 Chain K; UniProt 262–266 Chain L; UniProt 262–266 Fragment:TRAF-BINDING SEQUENCE Non-standard monomer:Yes (specific site not provided by mmCIF) TUMOR NECROSIS FACTOR RECEPTOR ASSOCIATED PROTEIN 2 × 6 (Q12933) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;pH 6;293 K;PEG4K, MES, PH 6.0, VAPOR DIFFUSION, temperature 293K Resolution 2.00 Å R-free 0.251
4 Protein heterocomplex Heteromer Protein × 12 PDB declaration: dodecameric(12) Consistent with protein copy count Chain G; UniProt 262–266 Chain H; UniProt 262–266 Chain I; UniProt 262–266 Chain J; UniProt 262–266 Chain K; UniProt 262–266 Chain L; UniProt 262–266 Fragment:TRAF-BINDING SEQUENCE Non-standard monomer:Yes (specific site not provided by mmCIF) TUMOR NECROSIS FACTOR RECEPTOR ASSOCIATED PROTEIN 2 × 6 (Q12933) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;pH 6;293 K;PEG4K, MES, PH 6.0, VAPOR DIFFUSION, temperature 293K Resolution 2.00 Å R-free 0.251

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.

7 other PDB entries and 11 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TNR4_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain G; PDBConstruct 2–6; UniProt 262–266 Author chain H; PDBConstruct 2–6; UniProt 262–266 Author chain I; PDBConstruct 2–6; UniProt 262–266 Author chain J; PDBConstruct 2–6; UniProt 262–266 Author chain K; PDBConstruct 2–6; UniProt 262–266 Author chain L; PDBConstruct 2–6; UniProt 262–266

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 1d0a

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1d0a
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1d0a
Deposition date deposition_date1999-09-09
Structure title titleSTRUCTURE OF TNF RECEPTOR ASSOCIATED FACTOR 2 (TRAF2) IN COMPLEX WITH A HUMAN OX40 PEPTIDE
Keywords keywordsB-SANDWICH, PROTEIN-PEPTIDE COMPLEX, APOPTOSIS; APOPTOSIS
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier41.47
Radius of gyration Rg (electron density) rg_electron40.74
Forward intensity I(0) i0185168000.00
Molecular weight molecular_weight113190.0 kDa
Excluded volume excluded_volume142460 ų
Envelope volume envelope_volume208090 ų
Hydration-shell volume shell_volume42382 ų
Envelope diameter envelope_diameter128.7
Shell Rg shell_rg47.59
Envelope Rg envelope_rg38.35
Shape Rg shape_rg40.73
Total Rg total_rg41.15
Total atoms total_atoms7968
Residues n_residues1038
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 dmax129.6
Rg (real space) rg_real41.38
Rg uncertainty (real space) rg_real_error0.99
I(0) (real space) i0_real1.8520e+08
I(0) uncertainty (real space) i0_real_error3.0880e+06
Rg (reciprocal space) rg_reciprocal41.47
I(0) (reciprocal space) i0_reciprocal185200000.0000
Solution quality estimate total_estimate0.8911
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary61.4
Skewness Skewness skewness0.046
Kurtosis Kurtosis kurtosis-0.805
Angular range angular_range— – 0.1900 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha18130000.0000
Real-space data points n_real_points39
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.917; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.987; Smooth: 0.845

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 18 domains

SCOP 2.08 (12 domains)

Domain ID domain_idd1d0aa1
Class classb — All beta proteins
Fold Fold foldb.8 — TRAF domain-like
Superfamily Superfamily superfamilyb.8.1 — TRAF domain-like
Family Family familyb.8.1.1 — MATH domain
Domain ID domain_idd1d0aa2
Class classh — Coiled coil proteins
Fold Fold foldh.1 — Parallel coiled-coil
Superfamily Superfamily superfamilyh.1.2 — Trimerization domain of TRAF
Family Family familyh.1.2.1 — Trimerization domain of TRAF
Domain ID domain_idd1d0ab1
Class classb — All beta proteins
Fold Fold foldb.8 — TRAF domain-like
Superfamily Superfamily superfamilyb.8.1 — TRAF domain-like
Family Family familyb.8.1.1 — MATH domain
Domain ID domain_idd1d0ab2
Class classh — Coiled coil proteins
Fold Fold foldh.1 — Parallel coiled-coil
Superfamily Superfamily superfamilyh.1.2 — Trimerization domain of TRAF
Family Family familyh.1.2.1 — Trimerization domain of TRAF
Domain ID domain_idd1d0ac1
Class classb — All beta proteins
Fold Fold foldb.8 — TRAF domain-like
Superfamily Superfamily superfamilyb.8.1 — TRAF domain-like
Family Family familyb.8.1.1 — MATH domain
Domain ID domain_idd1d0ac2
Class classh — Coiled coil proteins
Fold Fold foldh.1 — Parallel coiled-coil
Superfamily Superfamily superfamilyh.1.2 — Trimerization domain of TRAF
Family Family familyh.1.2.1 — Trimerization domain of TRAF
Domain ID domain_idd1d0ad1
Class classb — All beta proteins
Fold Fold foldb.8 — TRAF domain-like
Superfamily Superfamily superfamilyb.8.1 — TRAF domain-like
Family Family familyb.8.1.1 — MATH domain
Domain ID domain_idd1d0ad2
Class classh — Coiled coil proteins
Fold Fold foldh.1 — Parallel coiled-coil
Superfamily Superfamily superfamilyh.1.2 — Trimerization domain of TRAF
Family Family familyh.1.2.1 — Trimerization domain of TRAF
Domain ID domain_idd1d0ae1
Class classb — All beta proteins
Fold Fold foldb.8 — TRAF domain-like
Superfamily Superfamily superfamilyb.8.1 — TRAF domain-like
Family Family familyb.8.1.1 — MATH domain
Domain ID domain_idd1d0ae2
Class classh — Coiled coil proteins
Fold Fold foldh.1 — Parallel coiled-coil
Superfamily Superfamily superfamilyh.1.2 — Trimerization domain of TRAF
Family Family familyh.1.2.1 — Trimerization domain of TRAF
Domain ID domain_idd1d0af1
Class classb — All beta proteins
Fold Fold foldb.8 — TRAF domain-like
Superfamily Superfamily superfamilyb.8.1 — TRAF domain-like
Family Family familyb.8.1.1 — MATH domain
Domain ID domain_idd1d0af2
Class classh — Coiled coil proteins
Fold Fold foldh.1 — Parallel coiled-coil
Superfamily Superfamily superfamilyh.1.2 — Trimerization domain of TRAF
Family Family familyh.1.2.1 — Trimerization domain of TRAF

CATH v4.4 (6 domains)

Domain ID domain_id1d0aA00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology210 — Apoptosis, Tumor Necrosis Factor Receptor Associated Protein 2; Chain A
Homologous superfamily homologous superfamily10 — Apoptosis, Tumor Necrosis Factor Receptor Associated Protein 2; Chain A
Domain ID domain_id1d0aB00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology210 — Apoptosis, Tumor Necrosis Factor Receptor Associated Protein 2; Chain A
Homologous superfamily homologous superfamily10 — Apoptosis, Tumor Necrosis Factor Receptor Associated Protein 2; Chain A
Domain ID domain_id1d0aC00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology210 — Apoptosis, Tumor Necrosis Factor Receptor Associated Protein 2; Chain A
Homologous superfamily homologous superfamily10 — Apoptosis, Tumor Necrosis Factor Receptor Associated Protein 2; Chain A
Domain ID domain_id1d0aD00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology210 — Apoptosis, Tumor Necrosis Factor Receptor Associated Protein 2; Chain A
Homologous superfamily homologous superfamily10 — Apoptosis, Tumor Necrosis Factor Receptor Associated Protein 2; Chain A
Domain ID domain_id1d0aE00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology210 — Apoptosis, Tumor Necrosis Factor Receptor Associated Protein 2; Chain A
Homologous superfamily homologous superfamily10 — Apoptosis, Tumor Necrosis Factor Receptor Associated Protein 2; Chain A
Domain ID domain_id1d0aF00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology210 — Apoptosis, Tumor Necrosis Factor Receptor Associated Protein 2; Chain A
Homologous superfamily homologous superfamily10 — Apoptosis, Tumor Necrosis Factor Receptor Associated Protein 2; Chain A

8. Citations (2)

9. Files and Curves (10)