1tot

ZZ Domain of CBP- a Novel Fold for a Protein Interaction Module

Method: SOLUTION NMR Dmax: 29.5 Å Quality: EXCELLENT

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

CREB-binding protein

Mus musculus

UniProt P45481

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 1700–1751 Fragment:ZZ domain of murine CBP (residues 1700-1751) ZN ZINC ION × 2 SOLUTION NMR NMR measurement conditions:pH 6.8;298 K;Ionic strength (raw mmCIF value) 10 mM;Pressure ambient NMR sample composition:2.3 mM solutions in degassed 10 mM Tris-d11 pH 6.8, 200 M ZnCl2, 10 mM DTT-d10, 0.05% w/v sodium azide, 94 % H2O, 6 % D2O | 94 % H2O, 6 % D2O 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.

23 other PDB entries and 25 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CBP_MOUSE
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–52; UniProt 1700–1751

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 1tot

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1tot
Deposition date deposition_date2004-06-15
Structure title titleZZ Domain of CBP- a Novel Fold for a Protein Interaction Module
Keywords keywordsZinc Binding, CBP, TAZ2, TRANSFERASE; TRANSFERASE
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier9.62
Radius of gyration Rg (electron density) rg_electron9.97
Forward intensity I(0) i0281487000.00
Molecular weight molecular_weight126980.0 kDa
Excluded volume excluded_volume151960 ų
Envelope volume envelope_volume9680 ų
Hydration-shell volume shell_volume7935 ų
Envelope diameter envelope_diameter35.7
Shell Rg shell_rg15.98
Envelope Rg envelope_rg11.07
Shape Rg shape_rg9.98
Total Rg total_rg10.05
Total atoms total_atoms16560
Residues n_residues1040
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 dmax29.5
Rg (real space) rg_real9.55
Rg uncertainty (real space) rg_real_error0.29
I(0) (real space) i0_real2.8150e+08
I(0) uncertainty (real space) i0_real_error2.9830e+06
Rg (reciprocal space) rg_reciprocal9.55
I(0) (reciprocal space) i0_reciprocal281500000.0000
Solution quality estimate total_estimate0.9020
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary12.7
Skewness Skewness skewness0.041
Kurtosis Kurtosis kurtosis-0.385
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha42850.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.920; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.992; Smooth: 0.971

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1tota1
Class classg — Small proteins
Fold Fold foldg.44 — RING/U-box
Superfamily Superfamily superfamilyg.44.1 — RING/U-box
Family Family familyg.44.1.6 — ZZ domain

CATH v4.4 (1 domains)

Domain ID domain_id1totA00
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology60 — Wheat Germ Agglutinin (Isolectin 2); domain 1
Homologous superfamily homologous superfamily90 — Zinc finger, ZZ-type

8. Citations (1)

9. Files and Curves (10)