1bvo

DORSAL HOMOLOGUE GAMBIF1 BOUND TO DNA

Method: X-RAY DIFFRACTION Dmax: 76.6 Å Quality: GOOD

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

TRANSCRIPTION FACTOR GAMBIF1

Anopheles gambiae

UniProt Q17034

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–DNA Homooligomer Protein × 2 DNA 4 PDB declaration: hexameric(6) Consistent with all polymer counts Chain A; UniProt 48–222 Fragment:SPECIFICITY DOMAIN DNA DUPLEX × 2 DNA DUPLEX × 2 X-RAY DIFFRACTION X-ray crystallization conditions:pH 5.6;pH 5.6 Resolution 2.70 Å R-free 0.288

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 Q17034_ANOGA
Isoform
PDB entities 3
Chains and sequence ranges Author chain A; PDBConstruct 1–175; UniProt 48–222

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 1bvo

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1bvo
Deposition date deposition_date1998-09-16
Structure title titleDORSAL HOMOLOGUE GAMBIF1 BOUND TO DNA
Keywords keywords;TRANSCRIPTION FACTOR, REL PROTEIN, MORPHOGEN, IMMUNITY, DEVELOPMENT, INSECTS, COMPLEX (TRANSCRIPTION FACTOR-DNA), COMPLEX (TRANSCRIPTION FACTOR-DNA) complex ;; COMPLEX (TRANSCRIPTION FACTOR/DNA)
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier21.28
Radius of gyration Rg (electron density) rg_electron20.30
Forward intensity I(0) i020815200.00
Molecular weight molecular_weight28756.0 kDa
Excluded volume excluded_volume33335 ų
Envelope volume envelope_volume37166 ų
Hydration-shell volume shell_volume17037 ų
Envelope diameter envelope_diameter79.4
Shell Rg shell_rg24.83
Envelope Rg envelope_rg19.88
Shape Rg shape_rg20.26
Total Rg total_rg20.90
Total atoms total_atoms1986
Residues n_residues205
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 dmax76.6
Rg (real space) rg_real21.36
Rg uncertainty (real space) rg_real_error0.70
I(0) (real space) i0_real2.0820e+07
I(0) uncertainty (real space) i0_real_error2.8010e+05
Rg (reciprocal space) rg_reciprocal21.35
I(0) (reciprocal space) i0_reciprocal20820000.0000
Solution quality estimate total_estimate0.8564
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary24.8
Skewness Skewness skewness0.419
Kurtosis Kurtosis kurtosis-0.070
Angular range angular_range— – 0.3750 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha448000.0000
Real-space data points n_real_points69
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.749; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.893; Smooth: 0.988

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1bvoa_
Class classb — All beta proteins
Fold Fold foldb.2 — Common fold of diphtheria toxin/transcription factors/cytochrome f
Superfamily Superfamily superfamilyb.2.5 — p53-like transcription factors
Family Family familyb.2.5.3 — Rel/Dorsal transcription factors, DNA-binding domain

CATH v4.4 (1 domains)

Domain ID domain_id1bvoA00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily340 — Rel homology domain (RHD), DNA-binding domain

8. Citations (1)

9. Files and Curves (10)