1czy

CRYSTAL STRUCTURE OF THE COMPLEX BETWEEN THE TRAF DOMAIN OF HUMAN TRAF2 AND AN LMP1 BINDING PEPTIDE

Method: X-RAY DIFFRACTION Dmax: 81.0 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 334–501 Chain B; UniProt 334–501 Chain C; UniProt 334–501 Fragment:TRAF DOMAIN LATENT MEMBRANE PROTEIN 1 × 2 (P03230) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;pH 6;293 K;PEG4K, MES BUFFER, pH 6.00, VAPOR DIFFUSION, temperature 20K Resolution 2.00 Å R-free 0.245

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 1–168; UniProt 334–501 Author chain B; PDBConstruct 1–168; UniProt 334–501 Author chain C; PDBConstruct 1–168; UniProt 334–501

LATENT MEMBRANE PROTEIN 1

OrganismNot specified

UniProt P03230

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 204–210 Chain E; UniProt 204–210 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 6;293 K;PEG4K, MES BUFFER, pH 6.00, VAPOR DIFFUSION, temperature 20K Resolution 2.00 Å R-free 0.245

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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence
UniProt name LMP1_EBV
Isoform
PDB entities 2
Chains and sequence ranges Author chain D; PDBConstruct 2–8; UniProt 204–210 Author chain E; PDBConstruct 2–8; UniProt 204–210

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 1czy

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1czy
Deposition date deposition_date1999-09-07
Structure title titleCRYSTAL STRUCTURE OF THE COMPLEX BETWEEN THE TRAF DOMAIN OF HUMAN TRAF2 AND AN LMP1 BINDING PEPTIDE
Keywords keywordsBETA SANDWICH, PROTEIN-PEPTIDE COMPLEX, SIGNALING PROTEIN, APOPTOSIS; APOPTOSIS
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier27.09
Radius of gyration Rg (electron density) rg_electron25.81
Forward intensity I(0) i050970900.00
Molecular weight molecular_weight56217.0 kDa
Excluded volume excluded_volume70638 ų
Envelope volume envelope_volume86044 ų
Hydration-shell volume shell_volume28055 ų
Envelope diameter envelope_diameter77.5
Shell Rg shell_rg32.76
Envelope Rg envelope_rg25.32
Shape Rg shape_rg25.81
Total Rg total_rg26.60
Total atoms total_atoms3957
Residues n_residues518
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 dmax81.0
Rg (real space) rg_real26.97
Rg uncertainty (real space) rg_real_error0.39
I(0) (real space) i0_real5.0970e+07
I(0) uncertainty (real space) i0_real_error6.6680e+05
Rg (reciprocal space) rg_reciprocal27.01
I(0) (reciprocal space) i0_reciprocal50970000.0000
Solution quality estimate total_estimate0.9173
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary33.0
Skewness Skewness skewness0.115
Kurtosis Kurtosis kurtosis-0.731
Angular range angular_range— – 0.2950 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha7232000.0000
Real-space data points n_real_points60
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.979; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.985

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_idd1czya1
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_idd1czya2
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_idd1czyb1
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_idd1czyb2
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_idd1czyc1
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_idd1czyc2
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_id1czyA00
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_id1czyB00
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_id1czyC00
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)