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1bhi

STRUCTURE OF TRANSACTIVATION DOMAIN OF CRE-BP1/ATF-2, NMR, 20 STRUCTURES

Method: SOLUTION NMR Dmax: 48.2 Å Quality: REASONABLE
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1. Protein Identity and Related Structures Protein Identity & Related Structures

CRE-BP1

Homo sapiens

UniProt P15336

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 monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count Chain A； UniProt 1–38 Fragment：ZINC FINGER-LIKE SUBDOMAIN OF THE TRANSACTIVATION DOMAIN No other associated polymer SOLUTION NMR NMR measurement conditions：pH 6.3；300 K 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.

Other PDB Difference from Current Entry 1BHI Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
1T2K Structure Of The DNA Binding Domains Of IRF3, ATF-2 and Jun Bound To DNA Deposited 2004-04-21 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein–DNA Heteromer；Protein × 4 PDB declaration: hexameric
Chain D 336–396（61 aa） Fragment：bZip domain
Mutation：C351S No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；295 K；100 mM NaCacodylate, pH 6.5, 12.5% (w/v) PEG 6000, 400 mM NH4OAc, VAPOR DIFFUSION, HANGING DROP, temperature 295K
Resolution 3.00 Å R-free 0.296
4H36 Crystal Structure of JNK3 in Complex with ATF2 Peptide Deposited 2012-09-13 Different construct Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain B 48–55（8 aa） Fragment：UNP residues 48-55
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION；pH 5.5；294 K；0.2 M sodium chloride, 0.1 M Bis-Tris, 28-31% PEG3350, pH 5.5, VAPOR DIFFUSION, temperature 294K
Resolution 3.00 Å R-free 0.269
6ZQS Crystal structure of double-phosphorylated p38alpha with ATF2(83-102) Deposited 2020-07-10 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain B 83–102（20 aa）
Mutation：S90N 3FF 2-[(2,4-difluorophenyl)amino]-7-{[(2R)-2,3-dihydroxypropyl]oxy}-10,11-dihydro-5H-dibenzo[a,d][7]annulen-5-one × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；277 K；14% PEG 3350, 0.1 M cacodylate ph 6.5
Resolution 1.95 Å R-free 0.223
6ZR5 Crystal structure of JNK1 in complex with ATF2(19-58) Deposited 2020-07-10 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain C 20–58（39 aa）
Mutation：Q34R, H47R MG MAGNESIUM ION × 2 ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 1 ZN ZINC ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.8；277 K；10% PEG 20000, 20% PEG MME550, 0.03M MgCl2, 0.03M CaCl2, 0.1 M bicine/Trizma base, pH 8.8
Resolution 2.70 Å R-free 0.256
6ZR5 Crystal structure of JNK1 in complex with ATF2(19-58) Deposited 2020-07-10 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain D 20–58（39 aa）
Mutation：Q34R, H47R MG MAGNESIUM ION × 2 ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 1 ZN ZINC ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.8；277 K；10% PEG 20000, 20% PEG MME550, 0.03M MgCl2, 0.03M CaCl2, 0.1 M bicine/Trizma base, pH 8.8
Resolution 2.70 Å R-free 0.256
8YPE The crystal structure of inactive p38 complexed with a ATF2 from 46 to 80 Deposited 2024-03-16 Different construct Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain B 46–80（35 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；295 K；20% PEG 3350, 0.2M sodium citrate
Resolution 1.95 Å R-free 0.225
8YPF The crystal structure of inactive p38 complexed with a ATF2 from 46 to 90 Deposited 2024-03-16 Different construct Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain B 46–90（45 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；295 K；25% PEG1500, 0.1 M MMT buffer (DL-malic acid, MES monohydrate and Tris base, molar ratios 1:2:2) pH 7.0
Resolution 2.00 Å R-free 0.218
9Y0R Importin alpha 2 in complex with ATF2 basic region Deposited 2025-08-29 Different construct Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain B 352–378（27 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；296 K；sodium citrate 0.7 M, 0.1 M HEPES, 10 mM DTT, pH 7
Resolution 2.20 Å R-free 0.222

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

View Construct and Data Evidence
UniProt name ATF2_HUMAN
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 1–38； UniProt 1–38

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 1bhi

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1bhi
Deposition date deposition_date1998-06-09
Structure title titleSTRUCTURE OF TRANSACTIVATION DOMAIN OF CRE-BP1/ATF-2, NMR, 20 STRUCTURES
Keywords keywordsCRE BINDING PROTEIN, ATF-2, TRANSCRIPTIONAL ACTIVATION DOMAIN, ZN FINGER, DNA-BINDING REGULATORY PROTEIN; DNA-BINDING REGULATORY PROTEIN
Experimental Method methodSOLUTION NMR
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier10.88 Å
Radius of gyration Rg (electron density) rg_electron11.32 Å
Forward intensity I(0) i0121008000.00
Molecular weight molecular_weight86559.0 kDa
Excluded volume excluded_volume105980 ų
Envelope volume envelope_volume15834 ų
Hydration-shell volume shell_volume9711 ų
Envelope diameter envelope_diameter50.9 Å
Shell Rg shell_rg19.44 Å
Envelope Rg envelope_rg15.49 Å
Shape Rg shape_rg11.25 Å
Total Rg total_rg11.82 Å
Total atoms total_atoms11780
Residues n_residues760
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 Å−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
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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax48.2 Å
Rg (real space) rg_real11.04 Å
Rg uncertainty (real space) rg_real_error0.68 Å
I(0) (real space) i0_real1.2100e+08
I(0) uncertainty (real space) i0_real_error1.4860e+06
Rg (reciprocal space) rg_reciprocal11.03 Å
I(0) (reciprocal space) i0_reciprocal121000000.0000
Solution quality estimate total_estimate0.6997
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary11.0 Å
Skewness Skewness skewness0.657
Kurtosis Kurtosis kurtosis0.284
Angular range angular_range— – 0.5000 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha23790.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.340; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.073; Smooth: 0.999
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (1)

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7. Fold Classification (SCOP + CATH) 1 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1bhia_
Class classg — Small proteins
Fold Fold foldg.37 — beta-beta-alpha zinc fingers
Superfamily Superfamily superfamilyg.37.1 — beta-beta-alpha zinc fingers
Family Family familyg.37.1.1 — Classic zinc finger, C2H2
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8. Citations (4)

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9. Files and Curves (10)