3h11

Zymogen caspase-8:c-FLIPL protease domain complex

Method: X-RAY DIFFRACTION Dmax: 69.2 Å Quality: EXCELLENT

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

CASP8 and FADD-like apoptosis regulator

Homo sapiens

UniProt O15519

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 209–480 Not recorded Caspase-8 × 1 (Q14790) IETD aldehyde inhibitor × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 10.5;293 K;0.9 M sodium dihydrogen phosphate, 0.8 M dipotassium hydrogen phosphate, 0.1 M N-cyclohexyl-3-aminopropanesulfonic acid (CAPS), 0.2 M lithium sulfate, pH 10.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K Resolution 1.90 Å R-free 0.250

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.

15 other PDB entries and 15 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CFLAR_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–272; UniProt 209–480

Caspase-8

Homo sapiens

UniProt Q14790

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain B; UniProt 217–479 Mutation:D359A, D369A CASP8 and FADD-like apoptosis regulator × 1 (O15519) IETD aldehyde inhibitor × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 10.5;293 K;0.9 M sodium dihydrogen phosphate, 0.8 M dipotassium hydrogen phosphate, 0.1 M N-cyclohexyl-3-aminopropanesulfonic acid (CAPS), 0.2 M lithium sulfate, pH 10.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K Resolution 1.90 Å R-free 0.250

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.

33 other PDB entries and 45 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CASP8_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–263; UniProt 217–479

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 3h11

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3h11
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2. Structure Basics 2. Structure Basics

Entry ID entry_id3h11
Deposition date deposition_date2009-04-10
Structure title titleZymogen caspase-8:c-FLIPL protease domain complex
Keywords keywords;cell death, apoptosis, Caspase, Alternative splicing, Host-virus interaction, Polymorphism, Cytoplasm, Disease mutation, Hydrolase, Phosphoprotein, Protease, Thiol protease, Zymogen ;; APOPTOSIS
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier22.89
Radius of gyration Rg (electron density) rg_electron21.62
Forward intensity I(0) i043487600.00
Molecular weight molecular_weight51234.0 kDa
Excluded volume excluded_volume64085 ų
Envelope volume envelope_volume72905 ų
Hydration-shell volume shell_volume27254 ų
Envelope diameter envelope_diameter71.4
Shell Rg shell_rg29.18
Envelope Rg envelope_rg21.81
Shape Rg shape_rg21.61
Total Rg total_rg22.49
Total atoms total_atoms3595
Residues n_residues445
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 dmax69.2
Rg (real space) rg_real22.75
Rg uncertainty (real space) rg_real_error0.33
I(0) (real space) i0_real4.3490e+07
I(0) uncertainty (real space) i0_real_error4.7690e+05
Rg (reciprocal space) rg_reciprocal22.78
I(0) (reciprocal space) i0_reciprocal43490000.0000
Solution quality estimate total_estimate0.9090
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary28.8
Skewness Skewness skewness0.138
Kurtosis Kurtosis kurtosis-0.517
Angular range angular_range— – 0.3450 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha8477000.0000
Real-space data points n_real_points66
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.944; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.988; Smooth: 0.993

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd3h11a_
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.17 — Caspase-like
Superfamily Superfamily superfamilyc.17.1 — Caspase-like
Family Family familyc.17.1.1 — Caspase catalytic domain
Domain ID domain_idd3h11b_
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.17 — Caspase-like
Superfamily Superfamily superfamilyc.17.1 — Caspase-like
Family Family familyc.17.1.1 — Caspase catalytic domain

CATH v4.4 (2 domains)

Domain ID domain_id3h11A00
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily1460
Domain ID domain_id3h11B00
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily1460

8. Citations (1)

9. Files and Curves (10)