6isc

complex structure of mCD226-ecto and hCD155-D1

Method: X-RAY DIFFRACTION Dmax: 72.9 Å Quality: EXCELLENT

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

CD226 antigen

Mus musculus

UniProt Q8K4F0

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 heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 21–243 Not recorded Poliovirus receptor × 1 (P15151) NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;291 K;0.1 M Tris (pH 8.0), 0.15 M ammonium sulfate, and 15% (w/v) PEG4000 Resolution 2.20 Å R-free 0.265

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.

1 other PDB entries and 1 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CD226_MOUSE
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–223; UniProt 21–243

Poliovirus receptor

Homo sapiens

UniProt P15151

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 heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 28–145 Not recorded CD226 antigen × 1 (Q8K4F0) NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;291 K;0.1 M Tris (pH 8.0), 0.15 M ammonium sulfate, and 15% (w/v) PEG4000 Resolution 2.20 Å R-free 0.265

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.

12 other PDB entries and 41 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PVR_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–118; UniProt 28–145

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 6isc

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6isc
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id6isc
Deposition date deposition_date2018-11-16
Structure title titlecomplex structure of mCD226-ecto and hCD155-D1
Keywords keywordscomplex structure; mCD226; CD155; NK cell receptor, IMMUNE SYSTEM; IMMUNE SYSTEM
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier22.95
Radius of gyration Rg (electron density) rg_electron22.29
Forward intensity I(0) i025288400.00
Molecular weight molecular_weight38142.0 kDa
Excluded volume excluded_volume47658 ų
Envelope volume envelope_volume59383 ų
Hydration-shell volume shell_volume22547 ų
Envelope diameter envelope_diameter75.2
Shell Rg shell_rg28.69
Envelope Rg envelope_rg22.30
Shape Rg shape_rg22.27
Total Rg total_rg23.16
Total atoms total_atoms2683
Residues n_residues337
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 dmax72.9
Rg (real space) rg_real22.88
Rg uncertainty (real space) rg_real_error0.43
I(0) (real space) i0_real2.5290e+07
I(0) uncertainty (real space) i0_real_error3.2340e+05
Rg (reciprocal space) rg_reciprocal22.90
I(0) (reciprocal space) i0_reciprocal25290000.0000
Solution quality estimate total_estimate0.9070
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary28.1
Skewness Skewness skewness0.209
Kurtosis Kurtosis kurtosis-0.524
Angular range angular_range— – 0.3450 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha8586000.0000
Real-space data points n_real_points66
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.933; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.990

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd6iscb_
Class classb — All beta proteins
Fold Fold foldb.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamilyb.1.1 — Immunoglobulin
Family Family familyb.1.1.0 — automated matches

CATH v4.4 (1 domains)

Domain ID domain_id6iscB00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins

8. Citations (1)

9. Files and Curves (10)