1ahs

CRYSTAL STRUCTURE OF THE TOP DOMAIN OF AFRICAN HORSE SICKNESS VIRUS VP7

Method: X-RAY DIFFRACTION Dmax: 61.1 Å Quality: REASONABLE

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

AFRICAN HORSE SICKNESS VIRUS (SEROTYPE 4) VP7

OrganismNot specified

UniProt P36325

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 126–251 Chain B; UniProt 126–251 Chain C; UniProt 126–251 Fragment:TOP DOMAIN FRAGMENT No other associated polymer X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 2.30 Å

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 VP7_AHSV4
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–126; UniProt 126–251 Author chain B; PDBConstruct 1–126; UniProt 126–251 Author chain C; PDBConstruct 1–126; UniProt 126–251

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 1ahs

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1ahs
Deposition date deposition_date1996-03-18
Structure title titleCRYSTAL STRUCTURE OF THE TOP DOMAIN OF AFRICAN HORSE SICKNESS VIRUS VP7
Keywords keywordsCORE PROTEIN, GLYCOPROTEIN, COAT PROTEIN (VIRAL), 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_guinier21.04
Radius of gyration Rg (electron density) rg_electron19.94
Forward intensity I(0) i028034200.00
Molecular weight molecular_weight40252.0 kDa
Excluded volume excluded_volume50195 ų
Envelope volume envelope_volume59305 ų
Hydration-shell volume shell_volume24135 ų
Envelope diameter envelope_diameter63.6
Shell Rg shell_rg27.08
Envelope Rg envelope_rg20.07
Shape Rg shape_rg19.92
Total Rg total_rg20.88
Total atoms total_atoms2841
Residues n_residues378
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 dmax61.1
Rg (real space) rg_real20.88
Rg uncertainty (real space) rg_real_error0.30
I(0) (real space) i0_real2.8030e+07
I(0) uncertainty (real space) i0_real_error3.5920e+05
Rg (reciprocal space) rg_reciprocal20.91
I(0) (reciprocal space) i0_reciprocal28030000.0000
Solution quality estimate total_estimate0.6451
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary27.5
Skewness Skewness skewness0.069
Kurtosis Kurtosis kurtosis-0.553
Angular range angular_range— – 0.3800 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha6786000.0000
Real-space data points n_real_points70
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.957; Stabil: 1.000; Sysdev: 0.177; Positv: 1.000; Valcen: 0.979; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (3 domains)

Domain ID domain_idd1ahsa_
Class classb — All beta proteins
Fold Fold foldb.19 — Viral protein domain
Superfamily Superfamily superfamilyb.19.1 — Viral protein domain
Family Family familyb.19.1.1 — Top domain of virus capsid protein
Domain ID domain_idd1ahsb_
Class classb — All beta proteins
Fold Fold foldb.19 — Viral protein domain
Superfamily Superfamily superfamilyb.19.1 — Viral protein domain
Family Family familyb.19.1.1 — Top domain of virus capsid protein
Domain ID domain_idd1ahsc_
Class classb — All beta proteins
Fold Fold foldb.19 — Viral protein domain
Superfamily Superfamily superfamilyb.19.1 — Viral protein domain
Family Family familyb.19.1.1 — Top domain of virus capsid protein

CATH v4.4 (3 domains)

Domain ID domain_id1ahsA00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology120 — Jelly Rolls
Homologous superfamily homologous superfamily170
Domain ID domain_id1ahsB00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology120 — Jelly Rolls
Homologous superfamily homologous superfamily170
Domain ID domain_id1ahsC00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology120 — Jelly Rolls
Homologous superfamily homologous superfamily170

8. Citations (2)

9. Files and Curves (10)