2ljz

Structure of the C-terminal domain of HPV16 E6 oncoprotein

Method: SOLUTION NMR Dmax: 40.1 Å Quality: GOOD

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

Protein E6

Human papillomavirus

UniProt P03126

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 monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 87–158 Fragment:Zinc finger containing residues 87-158 Mutation:C80S, C97S, C111S, C140S ZN ZINC ION × 1 SOLUTION NMR NMR measurement conditions:pH 6.8;286 K;Ionic strength (raw mmCIF value) 50 mM NaCl;Pressure ambient NMR sample composition:1 mM E6, 90% H2O/10% D2O | 90% H2O/10% D2O NMR sample composition:1 mM [U-100% 13C; U-100% 15N] E6, 90% H2O/10% D2O | 90% H2O/10% D2O NMR sample composition:1 mM [U-100% 15N] E6, 90% H2O/10% D2O | 90% H2O/10% D2O Resolution not provided

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.

21 other PDB entries and 29 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name VE6_HPV16
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 4–75; UniProt 87–158

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 2ljz

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2ljz
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2ljz
Deposition date deposition_date2011-09-30
Structure title titleStructure of the C-terminal domain of HPV16 E6 oncoprotein
Keywords keywordsMETAL BINDING PROTEIN; METAL BINDING PROTEIN
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier11.80
Radius of gyration Rg (electron density) rg_electron11.75
Forward intensity I(0) i0534140000.00
Molecular weight molecular_weight179250.0 kDa
Excluded volume excluded_volume218360 ų
Envelope volume envelope_volume18472 ų
Hydration-shell volume shell_volume11465 ų
Envelope diameter envelope_diameter45.3
Shell Rg shell_rg19.49
Envelope Rg envelope_rg14.42
Shape Rg shape_rg11.71
Total Rg total_rg12.03
Total atoms total_atoms24880
Residues n_residues1500
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 dmax40.1
Rg (real space) rg_real11.77
Rg uncertainty (real space) rg_real_error0.36
I(0) (real space) i0_real5.3410e+08
I(0) uncertainty (real space) i0_real_error6.0850e+06
Rg (reciprocal space) rg_reciprocal11.78
I(0) (reciprocal space) i0_reciprocal534100000.0000
Solution quality estimate total_estimate0.7918
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary34.5
Skewness Skewness skewness0.288
Kurtosis Kurtosis kurtosis-0.210
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha127400.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.769; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.985; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd2ljza1
Class classg — Small proteins
Fold Fold foldg.90 — E6 C-terminal domain-like
Superfamily Superfamily superfamilyg.90.1 — E6 C-terminal domain-like
Family Family familyg.90.1.1 — E6 C-terminal domain-like
Domain ID domain_idd2ljza2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags

CATH v4.4 (1 domains)

Domain ID domain_id2ljzA00
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology240 — CRO Repressor
Homologous superfamily homologous superfamily40 — E6 early regulatory protein

8. Citations (1)

9. Files and Curves (10)