1f5w

DIMERIC STRUCTURE OF THE COXSACKIE VIRUS AND ADENOVIRUS RECEPTOR D1 DOMAIN

Method: X-RAY DIFFRACTION Dmax: 63.5 Å Quality: GOOD

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

COXSACKIE VIRUS AND ADENOVIRUS RECEPTOR

Homo sapiens

UniProt P78310

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 homooligomer Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 15–140 Chain B; UniProt 15–140 Fragment:D1 DOMAIN SO4 SULFATE ION × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 5.6;293 K;ammonium sulphate, sodium citrate, glycerol, pH 5.6, VAPOR DIFFUSION, SITTING DROP, temperature 293K Resolution 1.70 Å R-free 0.193
2 Protein homooligomer Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 15–140 Chain B; UniProt 15–140 Fragment:D1 DOMAIN SO4 SULFATE ION × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 5.6;293 K;ammonium sulphate, sodium citrate, glycerol, pH 5.6, VAPOR DIFFUSION, SITTING DROP, temperature 293K Resolution 1.70 Å R-free 0.193

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.

20 other PDB entries and 66 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CXAR_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–126; UniProt 15–140 Author chain B; PDBConstruct 1–126; UniProt 15–140

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 1f5w

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1f5w
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1f5w
Deposition date deposition_date2000-06-18
Structure title titleDIMERIC STRUCTURE OF THE COXSACKIE VIRUS AND ADENOVIRUS RECEPTOR D1 DOMAIN
Keywords keywordsimmunoglobulin V domain fold, symmetric dimer, Viral protein receptor; Viral protein receptor
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier19.75
Radius of gyration Rg (electron density) rg_electron18.83
Forward intensity I(0) i013063100.00
Molecular weight molecular_weight27450.0 kDa
Excluded volume excluded_volume34554 ų
Envelope volume envelope_volume40021 ų
Hydration-shell volume shell_volume18110 ų
Envelope diameter envelope_diameter65.4
Shell Rg shell_rg24.63
Envelope Rg envelope_rg18.96
Shape Rg shape_rg18.80
Total Rg total_rg19.80
Total atoms total_atoms1928
Residues n_residues245
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 dmax63.5
Rg (real space) rg_real19.67
Rg uncertainty (real space) rg_real_error0.46
I(0) (real space) i0_real1.3060e+07
I(0) uncertainty (real space) i0_real_error1.7640e+05
Rg (reciprocal space) rg_reciprocal19.69
I(0) (reciprocal space) i0_reciprocal13060000.0000
Solution quality estimate total_estimate0.8153
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary23.2
Skewness Skewness skewness0.261
Kurtosis Kurtosis kurtosis-0.311
Angular range angular_range— – 0.4050 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha2529000.0000
Real-space data points n_real_points72
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.866; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd1f5wa_
Class classb — All beta proteins
Fold Fold foldb.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamilyb.1.1 — Immunoglobulin
Family Family familyb.1.1.1 — V set domains (antibody variable domain-like)
Domain ID domain_idd1f5wb_
Class classb — All beta proteins
Fold Fold foldb.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamilyb.1.1 — Immunoglobulin
Family Family familyb.1.1.1 — V set domains (antibody variable domain-like)

CATH v4.4 (2 domains)

Domain ID domain_id1f5wA00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id1f5wB00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins

8. Citations (1)

9. Files and Curves (10)