6smv

Structure of HPV49 E6 protein in complex with MAML1 LxxLL motif

Method: X-RAY DIFFRACTION Dmax: 87.7 Å Quality: EXCELLENT

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

Maltose/maltodextrin-binding periplasmic protein,Protein E6,Mastermind-like protein 1

Homo sapiens

UniProt P0AEX9

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 Monomer Protein × 1 其他Polymer 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 26–392 Mutation:K84A,K240A,E360A,K363A,D364A,C1008A alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose × 1 ZN ZINC ION × 2 PEG DI(HYDROXYETHYL)ETHER × 1 X-RAY DIFFRACTION X-ray crystallization conditions:EVAPORATION;pH 6.8;277 K;Lithium Acetate 200mM, PEG 3350 22.5% Resolution 2.14 Å R-free 0.255

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.

366 other PDB entries and 491 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name MALE_ECOLI
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–367; UniProt 26–392

Maltose/maltodextrin-binding periplasmic protein,Protein E6,Mastermind-like protein 1

Homo sapiens

UniProt P36813

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 Monomer Protein × 1 其他Polymer 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 1–138 Mutation:K84A,K240A,E360A,K363A,D364A,C1008A alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose × 1 ZN ZINC ION × 2 PEG DI(HYDROXYETHYL)ETHER × 1 X-RAY DIFFRACTION X-ray crystallization conditions:EVAPORATION;pH 6.8;277 K;Lithium Acetate 200mM, PEG 3350 22.5% Resolution 2.14 Å R-free 0.255

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 VE6_HPV49
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 372–509; UniProt 1–138

Maltose/maltodextrin-binding periplasmic protein,Protein E6,Mastermind-like protein 1

Homo sapiens

UniProt Q92585

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 Monomer Protein × 1 其他Polymer 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 1003–1016 Mutation:K84A,K240A,E360A,K363A,D364A,C1008A alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose × 1 ZN ZINC ION × 2 PEG DI(HYDROXYETHYL)ETHER × 1 X-RAY DIFFRACTION X-ray crystallization conditions:EVAPORATION;pH 6.8;277 K;Lithium Acetate 200mM, PEG 3350 22.5% Resolution 2.14 Å R-free 0.255

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.

3 other PDB entries and 3 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name MAML1_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 525–538; UniProt 1003–1016

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 6smv

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6smv
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id6smv
Deposition date deposition_date2019-08-22
Structure title titleStructure of HPV49 E6 protein in complex with MAML1 LxxLL motif
Keywords keywordsHPV49 E6 protein, MAML1, 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_guinier27.19
Radius of gyration Rg (electron density) rg_electron26.34
Forward intensity I(0) i054309200.00
Molecular weight molecular_weight58421.0 kDa
Excluded volume excluded_volume73502 ų
Envelope volume envelope_volume90095 ų
Hydration-shell volume shell_volume29091 ų
Envelope diameter envelope_diameter92.5
Shell Rg shell_rg33.11
Envelope Rg envelope_rg26.26
Shape Rg shape_rg26.29
Total Rg total_rg27.25
Total atoms total_atoms4113
Residues n_residues525
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 dmax87.7
Rg (real space) rg_real27.19
Rg uncertainty (real space) rg_real_error0.62
I(0) (real space) i0_real5.4310e+07
I(0) uncertainty (real space) i0_real_error8.5380e+05
Rg (reciprocal space) rg_reciprocal27.19
I(0) (reciprocal space) i0_reciprocal54310000.0000
Solution quality estimate total_estimate0.9017
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary28.7
Skewness Skewness skewness0.308
Kurtosis Kurtosis kurtosis-0.491
Angular range angular_range— – 0.2900 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha12000000.0000
Real-space data points n_real_points59
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.922; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.991; Smooth: 0.962

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)