7d8p

CRTC1 pSer151 peptide in complex with 14-3-3 zeta

Method: X-RAY DIFFRACTION Dmax: 83.6 Å Quality: EXCELLENT

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

14-3-3 protein zeta/delta

Homo sapiens

UniProt P63104

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 heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 1–245 Chain B; UniProt 1–245 Not recorded CRTC1 pSer151 peptide × 2 (Q6UUV9) GOL GLYCEROL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;291 K;200mM Ammonium acetate, 100mM Bis-Tris (pH6.5), 25% (w/v) Polyethylene glycol 3350 Resolution 2.00 Å R-free 0.229

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.

73 other PDB entries and 88 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name 1433Z_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 21–265; UniProt 1–245 Author chain B; PDBConstruct 21–265; UniProt 1–245

CRTC1 pSer151 peptide

OrganismNot specified

UniProt Q6UUV9

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 heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain C; UniProt 146–156 Chain D; UniProt 146–156 Non-standard monomer:Yes (specific site not provided by mmCIF) 14-3-3 protein zeta/delta × 2 (P63104) GOL GLYCEROL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;291 K;200mM Ammonium acetate, 100mM Bis-Tris (pH6.5), 25% (w/v) Polyethylene glycol 3350 Resolution 2.00 Å R-free 0.229

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.

2 other PDB entries and 2 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CRTC1_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain C; PDBConstruct 1–11; UniProt 146–156 Author chain D; PDBConstruct 1–11; UniProt 146–156

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 7d8p

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7d8p
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7d8p
Deposition date deposition_date2020-10-08
Structure title titleCRTC1 pSer151 peptide in complex with 14-3-3 zeta
Keywords keywords14-3-3, CRTC1, protein complex, 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_guinier27.22
Radius of gyration Rg (electron density) rg_electron26.51
Forward intensity I(0) i050688600.00
Molecular weight molecular_weight54273.0 kDa
Excluded volume excluded_volume67499 ų
Envelope volume envelope_volume86530 ų
Hydration-shell volume shell_volume27224 ų
Envelope diameter envelope_diameter86.4
Shell Rg shell_rg33.87
Envelope Rg envelope_rg26.10
Shape Rg shape_rg26.52
Total Rg total_rg27.25
Total atoms total_atoms3804
Residues n_residues471
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 dmax83.6
Rg (real space) rg_real27.18
Rg uncertainty (real space) rg_real_error0.50
I(0) (real space) i0_real5.0690e+07
I(0) uncertainty (real space) i0_real_error7.3540e+05
Rg (reciprocal space) rg_reciprocal27.20
I(0) (reciprocal space) i0_reciprocal50690000.0000
Solution quality estimate total_estimate0.9137
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary30.3
Skewness Skewness skewness0.208
Kurtosis Kurtosis kurtosis-0.660
Angular range angular_range— – 0.2900 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha10100000.0000
Real-space data points n_real_points59
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.977; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.991; Smooth: 0.952

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 2 domains

CATH v4.4 (2 domains)

Domain ID domain_id7d8pA01
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology190 — Delta-Endotoxin; domain 1
Homologous superfamily homologous superfamily20 — 14-3-3 domain
Domain ID domain_id7d8pB01
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology190 — Delta-Endotoxin; domain 1
Homologous superfamily homologous superfamily20 — 14-3-3 domain

8. Citations (1)

9. Files and Curves (10)