6sqc

Crystal structure of complex between nuclear coactivator binding domain of CBP and [1040-1086]ACTR containing alpha-methylated Leu1055 and Leu1076

Method: X-RAY DIFFRACTION Dmax: 98.8 Å Quality: GOOD

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

Maltose/maltodextrin-binding periplasmic protein,CREB-binding protein

Homo sapiens

UniProt P0AEX9

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 2 其他Polymer 1 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 27–396 Not recorded Nuclear receptor coactivator 3 × 1 (Q9Y6Q9) alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose × 1 EDO 1,2-ETHANEDIOL × 1 ZN ZINC ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;298 K;20% PEG6000, 100 mM Tris pH 8 and 10 mM ZnCl2 Resolution 2.28 Å R-free 0.274

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.

366 other PDB entries and 491 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name MALE_ECOLI
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 2–371; UniProt 27–396

Maltose/maltodextrin-binding periplasmic protein,CREB-binding protein

Homo sapiens

UniProt Q92793

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 2 其他Polymer 1 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 2061–2112 Not recorded Nuclear receptor coactivator 3 × 1 (Q9Y6Q9) alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose × 1 EDO 1,2-ETHANEDIOL × 1 ZN ZINC ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;298 K;20% PEG6000, 100 mM Tris pH 8 and 10 mM ZnCl2 Resolution 2.28 Å R-free 0.274

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.

135 other PDB entries and 224 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CBP_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 373–424; UniProt 2061–2112

Nuclear receptor coactivator 3

OrganismNot specified

UniProt Q9Y6Q9

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 2 其他Polymer 1 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 975–1021 Non-standard monomer:Yes (specific site not provided by mmCIF) Maltose/maltodextrin-binding periplasmic protein,CREB-binding protein × 1 (P0AEX9,Q92793) alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose × 1 EDO 1,2-ETHANEDIOL × 1 ZN ZINC ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;298 K;20% PEG6000, 100 mM Tris pH 8 and 10 mM ZnCl2 Resolution 2.28 Å R-free 0.274

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 5 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name NCOA3_HUMAN
Isoform Q9Y6Q9-4
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–47; UniProt 975–1021

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 6sqc

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6sqc
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6sqc
Deposition date deposition_date2019-09-03
Structure title titleCrystal structure of complex between nuclear coactivator binding domain of CBP and [1040-1086]ACTR containing alpha-methylated Leu1055 and Leu1076
Keywords keywordscomplex, unnatural amino acid, PROTEIN BINDING; PROTEIN BINDING
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier26.08
Radius of gyration Rg (electron density) rg_electron25.31
Forward intensity I(0) i041928900.00
Molecular weight molecular_weight51033.0 kDa
Excluded volume excluded_volume64268 ų
Envelope volume envelope_volume77314 ų
Hydration-shell volume shell_volume26663 ų
Envelope diameter envelope_diameter100.9
Shell Rg shell_rg31.00
Envelope Rg envelope_rg25.75
Shape Rg shape_rg25.28
Total Rg total_rg26.08
Total atoms total_atoms3595
Residues n_residues463
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 dmax98.8
Rg (real space) rg_real26.24
Rg uncertainty (real space) rg_real_error0.95
I(0) (real space) i0_real4.1930e+07
I(0) uncertainty (real space) i0_real_error7.0390e+05
Rg (reciprocal space) rg_reciprocal26.19
I(0) (reciprocal space) i0_reciprocal41930000.0000
Solution quality estimate total_estimate0.8017
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary27.5
Skewness Skewness skewness0.590
Kurtosis Kurtosis kurtosis0.143
Angular range angular_range— – 0.3050 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha13470000.0000
Real-space data points n_real_points62
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.560; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.746; Smooth: 0.991

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

7. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

Domain ID domain_id6sqcA01
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology1630 — Creb-binding Protein; Chain: A
Homologous superfamily homologous superfamily10 — Nuclear receptor coactivator, CREB-bp-like, interlocking domain

8. Citations (1)

9. Files and Curves (10)