6sjv

Structure of HPV18 E6 oncoprotein in complex with mutant E6AP LxxLL motif

Method: X-RAY DIFFRACTION Dmax: 96.1 Å Quality: REASONABLE

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

Maltodextrin-binding protein,Protein E6,Ubiquitin-protein ligase E3A

Homo sapiens

UniProt A0A376KDN7

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 其他Polymer 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 27–392 Mutation:;K84A,K240A,E360A,K363A,D364A,F1049R,L2386F,E2393R,K84A,K240A,E360A,K363A,D364A,F1049R,L2386F,E2393R,K84A,K240A,E360A,K363A,D364A,F1049R,L2386F,E2393R ; alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose × 2 ZN ZINC ION × 4 X-RAY DIFFRACTION X-ray crystallization conditions:EVAPORATION;pH 6.5;298 K;Sodium Cacodylate 100 mM pH 6.5, PEG 8000 5%, 2-methyl-2,4-pentanediol 40% Resolution 2.03 Å R-free 0.242

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.

19 other PDB entries and 32 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0A376KDN7_ECOLX
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 2–367; UniProt 27–392

Maltodextrin-binding protein,Protein E6,Ubiquitin-protein ligase E3A

Homo sapiens

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 其他Polymer 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 1–152 Mutation:;K84A,K240A,E360A,K363A,D364A,F1049R,L2386F,E2393R,K84A,K240A,E360A,K363A,D364A,F1049R,L2386F,E2393R,K84A,K240A,E360A,K363A,D364A,F1049R,L2386F,E2393R ; alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose × 2 ZN ZINC ION × 4 X-RAY DIFFRACTION X-ray crystallization conditions:EVAPORATION;pH 6.5;298 K;Sodium Cacodylate 100 mM pH 6.5, PEG 8000 5%, 2-methyl-2,4-pentanediol 40% Resolution 2.03 Å R-free 0.242

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 372–523; UniProt 1–152

Maltodextrin-binding protein,Protein E6,Ubiquitin-protein ligase E3A

Homo sapiens

UniProt Q05086

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 其他Polymer 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 403–417 Mutation:;K84A,K240A,E360A,K363A,D364A,F1049R,L2386F,E2393R,K84A,K240A,E360A,K363A,D364A,F1049R,L2386F,E2393R,K84A,K240A,E360A,K363A,D364A,F1049R,L2386F,E2393R ; alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose × 2 ZN ZINC ION × 4 X-RAY DIFFRACTION X-ray crystallization conditions:EVAPORATION;pH 6.5;298 K;Sodium Cacodylate 100 mM pH 6.5, PEG 8000 5%, 2-methyl-2,4-pentanediol 40% Resolution 2.03 Å R-free 0.242

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 25 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name UBE3A_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 529–543; UniProt 403–417

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 6sjv

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id6sjv
Deposition date deposition_date2019-08-14
Structure title titleStructure of HPV18 E6 oncoprotein in complex with mutant E6AP LxxLL motif
Keywords keywordsHPV18 E6 protein, E6AP, LxxLL motif, VIRAL PROTEIN; VIRAL PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier29.35
Radius of gyration Rg (electron density) rg_electron28.60
Forward intensity I(0) i056468400.00
Molecular weight molecular_weight59413.0 kDa
Excluded volume excluded_volume74573 ų
Envelope volume envelope_volume97502 ų
Hydration-shell volume shell_volume29606 ų
Envelope diameter envelope_diameter102.1
Shell Rg shell_rg34.30
Envelope Rg envelope_rg29.17
Shape Rg shape_rg28.58
Total Rg total_rg29.21
Total atoms total_atoms4182
Residues n_residues529
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 dmax96.1
Rg (real space) rg_real29.44
Rg uncertainty (real space) rg_real_error0.70
I(0) (real space) i0_real5.6470e+07
I(0) uncertainty (real space) i0_real_error7.9630e+05
Rg (reciprocal space) rg_reciprocal29.40
I(0) (reciprocal space) i0_reciprocal56470000.0000
Solution quality estimate total_estimate0.6831
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary30.2
Skewness Skewness skewness0.381
Kurtosis Kurtosis kurtosis-0.486
Angular range angular_range— – 0.2700 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha8942000.0000
Real-space data points n_real_points55
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.899; Stabil: 1.000; Sysdev: 0.092; Positv: 1.000; Valcen: 0.955; Smooth: 0.948

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

Domain ID domain_id6sjvA01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology190 — D-Maltodextrin-Binding Protein; domain 2
Homologous superfamily homologous superfamily10 — Periplasmic binding protein-like II

8. Citations (1)

9. Files and Curves (10)