6zfg

14-3-3 zeta chimera with 18E6 and fusicoccin

Method: X-RAY DIFFRACTION Dmax: 85.8 Å Quality: EXCELLENT

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

14-3-3 protein zeta/delta,Protein E6

Human papillomavirus type 18

UniProt P06463

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 152–158 Chain B; UniProt 152–158 Non-standard monomer:Yes (specific site not provided by mmCIF) GOL GLYCEROL × 1 FSC FUSICOCCIN × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;277 K;19% PEG4000, 0.1M cacodylate, 20%glycerol as a cryoprotectant Resolution 1.85 Å R-free 0.219

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.

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

View Construct and Data Evidence
UniProt name VE6_HPV18
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 237–243; UniProt 152–158 Author chain B; PDBConstruct 237–243; UniProt 152–158

14-3-3 protein zeta/delta,Protein E6

Human papillomavirus type 18

UniProt P63104

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 1–229 Chain B; UniProt 1–229 Non-standard monomer:Yes (specific site not provided by mmCIF) GOL GLYCEROL × 1 FSC FUSICOCCIN × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;277 K;19% PEG4000, 0.1M cacodylate, 20%glycerol as a cryoprotectant Resolution 1.85 Å R-free 0.219

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.

73 other PDB entries and 88 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name 1433Z_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 4–232; UniProt 1–229 Author chain B; PDBConstruct 4–232; UniProt 1–229

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 6zfg

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6zfg
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6zfg
Deposition date deposition_date2020-06-17
Structure title title14-3-3 zeta chimera with 18E6 and fusicoccin
Keywords keywords14-3-3, HPV, E6 oncoprotein, PROTEIN BINDING; PROTEIN BINDING
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier28.37
Radius of gyration Rg (electron density) rg_electron27.11
Forward intensity I(0) i053205600.00
Molecular weight molecular_weight55688.0 kDa
Excluded volume excluded_volume69362 ų
Envelope volume envelope_volume93533 ų
Hydration-shell volume shell_volume28702 ų
Envelope diameter envelope_diameter83.2
Shell Rg shell_rg34.70
Envelope Rg envelope_rg26.58
Shape Rg shape_rg27.11
Total Rg total_rg27.95
Total atoms total_atoms3904
Residues n_residues479
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 dmax85.8
Rg (real space) rg_real28.24
Rg uncertainty (real space) rg_real_error0.49
I(0) (real space) i0_real5.3210e+07
I(0) uncertainty (real space) i0_real_error7.8710e+05
Rg (reciprocal space) rg_reciprocal28.28
I(0) (reciprocal space) i0_reciprocal53210000.0000
Solution quality estimate total_estimate0.9176
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary33.7
Skewness Skewness skewness0.085
Kurtosis Kurtosis kurtosis-0.763
Angular range angular_range— – 0.2800 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha5707000.0000
Real-space data points n_real_points57
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.982; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.998; Smooth: 0.982

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 5 domains

SCOP 2.08 (3 domains)

Domain ID domain_idd6zfga_
Class classa — All alpha proteins
Fold Fold folda.118 — alpha-alpha superhelix
Superfamily Superfamily superfamilya.118.7 — 14-3-3 protein
Family Family familya.118.7.1 — 14-3-3 protein
Domain ID domain_idd6zfgb1
Class classa — All alpha proteins
Fold Fold folda.118 — alpha-alpha superhelix
Superfamily Superfamily superfamilya.118.7 — 14-3-3 protein
Family Family familya.118.7.1 — 14-3-3 protein
Domain ID domain_idd6zfgb2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags

CATH v4.4 (2 domains)

Domain ID domain_id6zfgA01
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology190 — Delta-Endotoxin; domain 1
Homologous superfamily homologous superfamily20 — 14-3-3 domain
Domain ID domain_id6zfgB01
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology190 — Delta-Endotoxin; domain 1
Homologous superfamily homologous superfamily20 — 14-3-3 domain

8. Citations (1)

9. Files and Curves (10)