1czz

STRUCTURE OF TNF RECEPTOR ASSOCIATED FACTOR 2 IN COMPLEX WITH A 17-RESIDUE CD40 PEPTIDE

Method: X-RAY DIFFRACTION Dmax: 80.4 Å Quality: EXCELLENT

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 × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain A; UniProt 315–501 Chain B; UniProt 315–501 Chain C; UniProt 315–501 Fragment:TRAF DOMAIN CD 40 PEPTIDE × 2 (P25942) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;pH 5.6;293 K;PEG4K, MES, PH 5.6, VAPOR DIFFUSION, temperature 293K Resolution 2.70 Å R-free 0.267

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 26 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 1–187; UniProt 315–501 Author chain B; PDBConstruct 1–187; UniProt 315–501 Author chain C; PDBConstruct 1–187; UniProt 315–501

CD 40 PEPTIDE

OrganismNot specified

UniProt P25942

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 × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain D; UniProt 250–258 Chain E; UniProt 250–258 Fragment:TRAF2-BINDING REGION 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 5.6;293 K;PEG4K, MES, PH 5.6, VAPOR DIFFUSION, temperature 293K Resolution 2.70 Å R-free 0.267

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 34 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TNR5_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain D; PDBConstruct 2–10; UniProt 250–258 Author chain E; PDBConstruct 2–10; UniProt 250–258

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 1czz

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1czz
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id1czz
Deposition date deposition_date1999-09-07
Structure title titleSTRUCTURE OF TNF RECEPTOR ASSOCIATED FACTOR 2 IN COMPLEX WITH A 17-RESIDUE CD40 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_guinier28.20
Radius of gyration Rg (electron density) rg_electron26.90
Forward intensity I(0) i062103600.00
Molecular weight molecular_weight61700.0 kDa
Excluded volume excluded_volume77334 ų
Envelope volume envelope_volume96871 ų
Hydration-shell volume shell_volume30190 ų
Envelope diameter envelope_diameter79.5
Shell Rg shell_rg33.85
Envelope Rg envelope_rg26.65
Shape Rg shape_rg26.90
Total Rg total_rg27.63
Total atoms total_atoms4340
Residues n_residues577
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 dmax80.4
Rg (real space) rg_real27.98
Rg uncertainty (real space) rg_real_error0.43
I(0) (real space) i0_real6.2100e+07
I(0) uncertainty (real space) i0_real_error8.8600e+05
Rg (reciprocal space) rg_reciprocal28.05
I(0) (reciprocal space) i0_reciprocal62110000.0000
Solution quality estimate total_estimate0.9171
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary37.3
Skewness Skewness skewness-0.005
Kurtosis Kurtosis kurtosis-0.738
Angular range angular_range— – 0.2800 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha5851000.0000
Real-space data points n_real_points57
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.993; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.998; Smooth: 0.941

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 9 domains

SCOP 2.08 (6 domains)

Domain ID domain_idd1czza1
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_idd1czza2
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_idd1czzb1
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_idd1czzb2
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_idd1czzc1
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_idd1czzc2
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 (3 domains)

Domain ID domain_id1czzA00
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_id1czzB00
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_id1czzC00
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)