1dbd

E2 DNA-BINDING DOMAIN FROM PAPILLOMAVIRUS BPV-1

Method: SOLUTION NMR Dmax: 65.5 Å Quality: GOOD

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

REGULATORY PROTEIN E2

Bovine papillomavirus type 1

UniProt P03122

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 311–410 Chain B; UniProt 311–410 Fragment:DNA-BINDING DOMAIN No other associated polymer SOLUTION NMR NMR measurement conditions:pH 5.75;308.3 K;Ionic strength (raw mmCIF value) 0.1;Pressure 1 Resolution not provided

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.

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

View Construct and Data Evidence
UniProt name VE2_BPV1
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–100; UniProt 311–410 Author chain B; PDBConstruct 1–100; UniProt 311–410

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 1dbd

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1dbd
Deposition date deposition_date1999-05-21
Structure title titleE2 DNA-BINDING DOMAIN FROM PAPILLOMAVIRUS BPV-1
Keywords keywordsDNA-BINDING DOMAIN, GENE REGULATION; GENE REGULATION
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier19.09
Radius of gyration Rg (electron density) rg_electron17.82
Forward intensity I(0) i010087300.00
Molecular weight molecular_weight22480.0 kDa
Excluded volume excluded_volume27807 ų
Envelope volume envelope_volume35639 ų
Hydration-shell volume shell_volume17052 ų
Envelope diameter envelope_diameter65.9
Shell Rg shell_rg23.63
Envelope Rg envelope_rg18.17
Shape Rg shape_rg17.78
Total Rg total_rg18.90
Total atoms total_atoms1584
Residues n_residues200
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 dmax65.5
Rg (real space) rg_real19.01
Rg uncertainty (real space) rg_real_error0.39
I(0) (real space) i0_real1.0090e+07
I(0) uncertainty (real space) i0_real_error1.2090e+05
Rg (reciprocal space) rg_reciprocal19.03
I(0) (reciprocal space) i0_reciprocal10090000.0000
Solution quality estimate total_estimate0.8657
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary23.6
Skewness Skewness skewness0.242
Kurtosis Kurtosis kurtosis-0.277
Angular range angular_range— – 0.4150 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1563000.0000
Real-space data points n_real_points73
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.752; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.997; Smooth: 0.997

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd1dbda_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.58 — Ferredoxin-like
Superfamily Superfamily superfamilyd.58.8 — Viral DNA-binding domain
Family Family familyd.58.8.1 — Viral DNA-binding domain
Domain ID domain_idd1dbdb_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.58 — Ferredoxin-like
Superfamily Superfamily superfamilyd.58.8 — Viral DNA-binding domain
Family Family familyd.58.8.1 — Viral DNA-binding domain

CATH v4.4 (2 domains)

Domain ID domain_id1dbdA00
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology70 — Alpha-Beta Plaits
Homologous superfamily homologous superfamily330 — RRM (RNA recognition motif) domain
Domain ID domain_id1dbdB00
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology70 — Alpha-Beta Plaits
Homologous superfamily homologous superfamily330 — RRM (RNA recognition motif) domain

8. Citations (1)

9. Files and Curves (10)