1uxe

ADENOVIRUS AD37 FIBRE HEAD

Method: X-RAY DIFFRACTION Dmax: 71.4 Å Quality: EXCELLENT

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

FIBER PROTEIN

HUMAN ADENOVIRUS TYPE 37

UniProt Q64823

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 172–365 Chain B; UniProt 172–365 Chain C; UniProt 172–365 Fragment:HEAD DOMAIN RESIDUES 172-365 Mutation:YES ZN ZINC ION × 3 ACT ACETATE ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:pH 7.5;RESERVOIR: 24 % PEG8000, 50 MM ZINC ACETATE, 100 MM HEPES, PH 7.5 PROTEIN: 30 MM TRIS-HCL, PH 7.5, 150 MM NACL Resolution 2.00 Å R-free 0.241

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.

13 other PDB entries and 16 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name Q64823
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–194; UniProt 172–365 Author chain B; PDBConstruct 1–194; UniProt 172–365 Author chain C; PDBConstruct 1–194; UniProt 172–365

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 1uxe

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1uxe
Deposition date deposition_date2004-02-24
Structure title titleADENOVIRUS AD37 FIBRE HEAD
Keywords keywordsVIRAL PROTEIN, ADENOVIRUS, AD37, FIBRE, RECEPTOR, SIALIC ACID, NEURAMINIC ACID, CD46, DAF, CONJUNCTIVITIS; VIRAL PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier24.62
Radius of gyration Rg (electron density) rg_electron23.17
Forward intensity I(0) i059757900.00
Molecular weight molecular_weight61911.0 kDa
Excluded volume excluded_volume78138 ų
Envelope volume envelope_volume91394 ų
Hydration-shell volume shell_volume31480 ų
Envelope diameter envelope_diameter74.4
Shell Rg shell_rg31.43
Envelope Rg envelope_rg23.35
Shape Rg shape_rg23.12
Total Rg total_rg24.27
Total atoms total_atoms4360
Residues n_residues550
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 dmax71.4
Rg (real space) rg_real24.39
Rg uncertainty (real space) rg_real_error0.33
I(0) (real space) i0_real5.9760e+07
I(0) uncertainty (real space) i0_real_error7.6380e+05
Rg (reciprocal space) rg_reciprocal24.45
I(0) (reciprocal space) i0_reciprocal59760000.0000
Solution quality estimate total_estimate0.9107
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary69.1
Skewness Skewness skewness0.033
Kurtosis Kurtosis kurtosis-0.558
Angular range angular_range— – 0.3200 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha10070000.0000
Real-space data points n_real_points64
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.962; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.973; Smooth: 0.977

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (3 domains)

Domain ID domain_idd1uxea_
Class classb — All beta proteins
Fold Fold foldb.21 — Virus attachment protein globular domain
Superfamily Superfamily superfamilyb.21.1 — Virus attachment protein globular domain
Family Family familyb.21.1.1 — Adenovirus fiber protein 'knob' domain
Domain ID domain_idd1uxeb_
Class classb — All beta proteins
Fold Fold foldb.21 — Virus attachment protein globular domain
Superfamily Superfamily superfamilyb.21.1 — Virus attachment protein globular domain
Family Family familyb.21.1.1 — Adenovirus fiber protein 'knob' domain
Domain ID domain_idd1uxec_
Class classb — All beta proteins
Fold Fold foldb.21 — Virus attachment protein globular domain
Superfamily Superfamily superfamilyb.21.1 — Virus attachment protein globular domain
Family Family familyb.21.1.1 — Adenovirus fiber protein 'knob' domain

CATH v4.4 (3 domains)

Domain ID domain_id1uxeA00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology90 — Adenovirus Type 5 Fiber Protein (Receptor Binding Domain)
Homologous superfamily homologous superfamily10 — Adenovirus pIV-related, attachment domain
Domain ID domain_id1uxeB00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology90 — Adenovirus Type 5 Fiber Protein (Receptor Binding Domain)
Homologous superfamily homologous superfamily10 — Adenovirus pIV-related, attachment domain
Domain ID domain_id1uxeC00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology90 — Adenovirus Type 5 Fiber Protein (Receptor Binding Domain)
Homologous superfamily homologous superfamily10 — Adenovirus pIV-related, attachment domain

8. Citations (1)

9. Files and Curves (10)