1p35

CRYSTAL STRUCTURE OF BACULOVIRUS P35

Method: X-RAY DIFFRACTION Dmax: 133.8 Å Quality: REASONABLE

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

P35

Autographa californica nucleopolyhedrovirus

UniProt P08160

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 2–299 Chain C; UniProt 2–299 Not recorded PO4 PHOSPHATE ION × 2 EDO 1,2-ETHANEDIOL × 2 X-RAY DIFFRACTION X-ray crystallization conditions:pH 7;pH 7.0 Resolution 2.20 Å R-free 0.262
2 Protein homooligomer Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 2–299 Not recorded PO4 PHOSPHATE ION × 2 EDO 1,2-ETHANEDIOL × 2 X-RAY DIFFRACTION X-ray crystallization conditions:pH 7;pH 7.0 Resolution 2.20 Å R-free 0.262

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.

4 other PDB entries and 8 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name VP35_NPVAC
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–298; UniProt 2–299 Author chain B; PDBConstruct 1–298; UniProt 2–299 Author chain C; PDBConstruct 1–298; UniProt 2–299

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 1p35

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1p35
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1p35
Deposition date deposition_date1998-09-18
Structure title titleCRYSTAL STRUCTURE OF BACULOVIRUS P35
Keywords keywordsAPOPTOSIS, P35, CELL DEATH, BACULOVIRUS; APOPTOSIS
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier38.81
Radius of gyration Rg (electron density) rg_electron38.88
Forward intensity I(0) i0159489000.00
Molecular weight molecular_weight103280.0 kDa
Excluded volume excluded_volume129820 ų
Envelope volume envelope_volume182640 ų
Hydration-shell volume shell_volume41336 ų
Envelope diameter envelope_diameter142.7
Shell Rg shell_rg41.93
Envelope Rg envelope_rg38.61
Shape Rg shape_rg38.87
Total Rg total_rg39.12
Total atoms total_atoms7271
Residues n_residues892
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 dmax133.8
Rg (real space) rg_real39.15
Rg uncertainty (real space) rg_real_error1.05
I(0) (real space) i0_real1.5950e+08
I(0) uncertainty (real space) i0_real_error2.9490e+06
Rg (reciprocal space) rg_reciprocal38.95
I(0) (reciprocal space) i0_reciprocal159500000.0000
Solution quality estimate total_estimate0.6235
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary32.6
Skewness Skewness skewness0.460
Kurtosis Kurtosis kurtosis-0.384
Angular range angular_range— – 0.2050 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha36580000.0000
Real-space data points n_real_points42
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.794; Stabil: 1.000; Sysdev: 0.035; Positv: 1.000; Valcen: 0.805; Smooth: 0.809

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_idd1p35a_
Class classb — All beta proteins
Fold Fold foldb.28 — Baculovirus p35 protein
Superfamily Superfamily superfamilyb.28.1 — Baculovirus p35 protein
Family Family familyb.28.1.1 — Baculovirus p35 protein
Domain ID domain_idd1p35b_
Class classb — All beta proteins
Fold Fold foldb.28 — Baculovirus p35 protein
Superfamily Superfamily superfamilyb.28.1 — Baculovirus p35 protein
Family Family familyb.28.1.1 — Baculovirus p35 protein
Domain ID domain_idd1p35c_
Class classb — All beta proteins
Fold Fold foldb.28 — Baculovirus p35 protein
Superfamily Superfamily superfamilyb.28.1 — Baculovirus p35 protein
Family Family familyb.28.1.1 — Baculovirus p35 protein

CATH v4.4 (3 domains)

Domain ID domain_id1p35A00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology250 — Baculovirus p35
Homologous superfamily homologous superfamily10 — Baculovirus p35
Domain ID domain_id1p35B00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology250 — Baculovirus p35
Homologous superfamily homologous superfamily10 — Baculovirus p35
Domain ID domain_id1p35C00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology250 — Baculovirus p35
Homologous superfamily homologous superfamily10 — Baculovirus p35

8. Citations (1)

9. Files and Curves (10)