1h8a

CRYSTAL STRUCTURE OF TERNARY PROTEIN-DNA COMPLEX3

Method: X-RAY DIFFRACTION Dmax: 104.8 Å Quality: GOOD

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

CAAT/ENHANCER BINDING PROTEIN BETA

HOMO SAPIENS

UniProt P17676

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 Heteromer Protein × 3 DNA 2 PDB declaration: pentameric(5) Consistent with all polymer counts Chain A; UniProt 259–336 Chain B; UniProt 259–336 Fragment:RESIDUES 259-336 MYB TRANSFORMING PROTEIN × 1 (P01104) ;DNA(5'-(*GP*AP*TP*GP*TP*GP*GP*CP*GP*CP*AP* AP*TP*CP*CP*TP*TP*AP*AP*CP*GP*GP*AP*CP*TP*G)-3') ; × 1 ;DNA(5'-(*CP*CP*AP*GP*TP*CP*CP*GP*TP*TP*AP* AP*GP*GP*AP*TP*TP*GP*CP*GP*CP*CP*AP*CP*AP*T)-3') ; × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6;297 K;0.04 M MAGNESIUM CHLORIDE, 20% V/V MPD, 0.05 M SODIUM CACODYLATE BUFFER PH 6.0 AT 24 DEGREES C Resolution 2.23 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.

15 other PDB entries and 17 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CEBB_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–78; UniProt 259–336 Author chain B; PDBConstruct 1–78; UniProt 259–336

MYB TRANSFORMING PROTEIN

AVIAN MYELOBLASTOSIS VIRUS

UniProt P01104

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 Heteromer Protein × 3 DNA 2 PDB declaration: pentameric(5) Consistent with all polymer counts Chain C; UniProt 1–122 Fragment:RESIDUES 1-128 CAAT/ENHANCER BINDING PROTEIN BETA × 2 (P17676) ;DNA(5'-(*GP*AP*TP*GP*TP*GP*GP*CP*GP*CP*AP* AP*TP*CP*CP*TP*TP*AP*AP*CP*GP*GP*AP*CP*TP*G)-3') ; × 1 ;DNA(5'-(*CP*CP*AP*GP*TP*CP*CP*GP*TP*TP*AP* AP*GP*GP*AP*TP*TP*GP*CP*GP*CP*CP*AP*CP*AP*T)-3') ; × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6;297 K;0.04 M MAGNESIUM CHLORIDE, 20% V/V MPD, 0.05 M SODIUM CACODYLATE BUFFER PH 6.0 AT 24 DEGREES C Resolution 2.23 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 MYB_AVIMB
Isoform
PDB entities 2
Chains and sequence ranges Author chain C; PDBConstruct 7–128; UniProt 1–122

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 1h8a

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1h8a
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id1h8a
Deposition date deposition_date2001-01-31
Structure title titleCRYSTAL STRUCTURE OF TERNARY PROTEIN-DNA COMPLEX3
Keywords keywords;TRANSCRIPTION/DNA, PROTEIN-DNA COMPLEX, TRANSCRIPTION REGULATION, BZIP, V-MYB, C-MYB, AMV, C/EBP, AVIAN MYELOBLASTOSIS VIRUS, TRANSFORMING PROTEIN, TRANSCRIPTION-DNA complex ;; TRANSCRIPTION/DNA
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier29.75
Radius of gyration Rg (electron density) rg_electron30.67
Forward intensity I(0) i052404900.00
Molecular weight molecular_weight45041.0 kDa
Excluded volume excluded_volume51442 ų
Envelope volume envelope_volume76715 ų
Hydration-shell volume shell_volume22853 ų
Envelope diameter envelope_diameter111.9
Shell Rg shell_rg34.38
Envelope Rg envelope_rg30.84
Shape Rg shape_rg30.69
Total Rg total_rg30.94
Total atoms total_atoms3105
Residues n_residues292
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 dmax104.8
Rg (real space) rg_real29.97
Rg uncertainty (real space) rg_real_error1.08
I(0) (real space) i0_real5.2400e+07
I(0) uncertainty (real space) i0_real_error8.5440e+05
Rg (reciprocal space) rg_reciprocal29.88
I(0) (reciprocal space) i0_reciprocal52400000.0000
Solution quality estimate total_estimate0.8225
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary23.7
Skewness Skewness skewness0.399
Kurtosis Kurtosis kurtosis-0.578
Angular range angular_range— – 0.2650 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha3137000.0000
Real-space data points n_real_points54
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.725; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.559; Smooth: 0.955

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 8 domains

SCOP 2.08 (4 domains)

Domain ID domain_idd1h8aa_
Class classh — Coiled coil proteins
Fold Fold foldh.1 — Parallel coiled-coil
Superfamily Superfamily superfamilyh.1.3 — Leucine zipper domain
Family Family familyh.1.3.1 — Leucine zipper domain
Domain ID domain_idd1h8ab_
Class classh — Coiled coil proteins
Fold Fold foldh.1 — Parallel coiled-coil
Superfamily Superfamily superfamilyh.1.3 — Leucine zipper domain
Family Family familyh.1.3.1 — Leucine zipper domain
Domain ID domain_idd1h8ac1
Class classa — All alpha proteins
Fold Fold folda.4 — DNA/RNA-binding 3-helical bundle
Superfamily Superfamily superfamilya.4.1 — Homeodomain-like
Family Family familya.4.1.3 — Myb/SANT domain
Domain ID domain_idd1h8ac2
Class classa — All alpha proteins
Fold Fold folda.4 — DNA/RNA-binding 3-helical bundle
Superfamily Superfamily superfamilya.4.1 — Homeodomain-like
Family Family familya.4.1.3 — Myb/SANT domain

CATH v4.4 (4 domains)

Domain ID domain_id1h8aA00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology5 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily170
Domain ID domain_id1h8aB00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology5 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily170
Domain ID domain_id1h8aC01
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology10 — Arc Repressor Mutant, subunit A
Homologous superfamily homologous superfamily60 — Homeodomain-like
Domain ID domain_id1h8aC02
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology10 — Arc Repressor Mutant, subunit A
Homologous superfamily homologous superfamily60 — Homeodomain-like

8. Citations (4)

9. Files and Curves (10)