9ejw

MCMV immunoevasin m11 binding murine CD44

Method: X-RAY DIFFRACTION Dmax: 74.4 Å Quality: GOOD

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

CD44 antigen

Mus musculus

UniProt P15379

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Other combination Heteromer Protein × 2 其他Polymer 3 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 23–174 Fragment:UNP residues 23-174 M11 protein × 1 (A8E1J2) beta-D-galactopyranose-(1-3)-2-acetamido-2-deoxy-alpha-D-galactopyranose × 1 ;alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-3)-alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose ; × 1 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 1 SO4 SULFATE ION × 2 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 CYS CYSTEINE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8.5;293 K;30% w/v PEG3000, 0.2 M lithium sulfate, 0.1 M Tris-HCl, pH 8.5 Resolution 1.40 Å R-free 0.202

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.

52 other PDB entries and 52 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CD44_MOUSE
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 3–154; UniProt 23–174

M11 protein

Murid betaherpesvirus 1

UniProt A8E1J2

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Other combination Heteromer Protein × 2 其他Polymer 3 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 28–165 Fragment:UNP residues 28-165 CD44 antigen × 1 (P15379) beta-D-galactopyranose-(1-3)-2-acetamido-2-deoxy-alpha-D-galactopyranose × 1 ;alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-3)-alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose ; × 1 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 1 SO4 SULFATE ION × 2 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 CYS CYSTEINE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8.5;293 K;30% w/v PEG3000, 0.2 M lithium sulfate, 0.1 M Tris-HCl, pH 8.5 Resolution 1.40 Å R-free 0.202

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 A8E1J2_MUHVK
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 3–140; UniProt 28–165

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 9ejw

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9ejw
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9ejw
Deposition date deposition_date2024-11-29
Structure title titleMCMV immunoevasin m11 binding murine CD44
Keywords keywordsImmunoevasin, Complex, Cytomegalovirus, 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_guinier22.51
Radius of gyration Rg (electron density) rg_electron21.82
Forward intensity I(0) i020819300.00
Molecular weight molecular_weight33598.0 kDa
Excluded volume excluded_volume41501 ų
Envelope volume envelope_volume50722 ų
Hydration-shell volume shell_volume19855 ų
Envelope diameter envelope_diameter76.1
Shell Rg shell_rg27.74
Envelope Rg envelope_rg21.99
Shape Rg shape_rg21.82
Total Rg total_rg22.57
Total atoms total_atoms2349
Residues n_residues286
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 dmax74.4
Rg (real space) rg_real22.51
Rg uncertainty (real space) rg_real_error0.45
I(0) (real space) i0_real2.0820e+07
I(0) uncertainty (real space) i0_real_error2.9030e+05
Rg (reciprocal space) rg_reciprocal22.51
I(0) (reciprocal space) i0_reciprocal20820000.0000
Solution quality estimate total_estimate0.8922
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary22.5
Skewness Skewness skewness0.306
Kurtosis Kurtosis kurtosis-0.508
Angular range angular_range— – 0.3550 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha5779000.0000
Real-space data points n_real_points67
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.873; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.977; Smooth: 0.997

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (9)

8. Citations (1)

9. Files and Curves (10)