1rg6

Solution structure of the C-terminal domain of p63

Method: SOLUTION NMR Dmax: 44.9 Å Quality: GOOD

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

second splice variant p63

Homo sapiens

UniProt Q9H3D4

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 501–575 Fragment:C-terminal domain (residues 501-575) No other associated polymer SOLUTION NMR NMR measurement conditions:pH 6;298 K;Ionic strength (raw mmCIF value) 150mM NaCl;Pressure ambient NMR measurement conditions:pH 6;298 K;Ionic strength (raw mmCIF value) 150mM NaCl;Pressure ambient NMR measurement conditions:pH 6;298 K;Ionic strength (raw mmCIF value) 150mM NaCl;Pressure ambient NMR measurement conditions:pH 6;298 K;Ionic strength (raw mmCIF value) 150mM NaCl;Pressure ambient NMR sample composition:0.75mM p63 U-15N, 25mM sodium posphate, 150mM sodium chloride, 1mM AEBSF, 3mM DTT, 95% H20, 5%D2O | 95% H20, 5%D2O NMR sample composition:0.25mM p63 U-15N U-13C, 25mM sodium posphate, 150mM sodium chloride, 1mM AEBSF, 3mM DTT, 95% H20, 5%D2O | 95% H20, 5%D2O NMR sample composition:0.25mM p63 U-15N U-13C, 25mM sodium posphate, 150mM sodium chloride, 1mM AEBSF, 3mM DTT, 100% D2O | 100% D2O NMR sample composition:0.75mM p63 U-15N, 25mM sodium posphate, 150mM sodium chloride, 1mM AEBSF, 3mM DTT, phage | phage 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.

25 other PDB entries and 36 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name P73L_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–75; UniProt 501–575

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 1rg6

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1rg6
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1rg6
Deposition date deposition_date2003-11-11
Structure title titleSolution structure of the C-terminal domain of p63
Keywords keywordsP73 SAM-LIKE DOMAIN, GENE REGULATION; GENE REGULATION
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier11.99
Radius of gyration Rg (electron density) rg_electron11.62
Forward intensity I(0) i0330702000.00
Molecular weight molecular_weight154840.0 kDa
Excluded volume excluded_volume193780 ų
Envelope volume envelope_volume17571 ų
Hydration-shell volume shell_volume11248 ų
Envelope diameter envelope_diameter45.6
Shell Rg shell_rg19.12
Envelope Rg envelope_rg14.03
Shape Rg shape_rg11.62
Total Rg total_rg11.79
Total atoms total_atoms21420
Residues n_residues1340
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 dmax44.9
Rg (real space) rg_real11.91
Rg uncertainty (real space) rg_real_error0.36
I(0) (real space) i0_real3.3070e+08
I(0) uncertainty (real space) i0_real_error3.5960e+06
Rg (reciprocal space) rg_reciprocal11.91
I(0) (reciprocal space) i0_reciprocal330700000.0000
Solution quality estimate total_estimate0.7548
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary37.5
Skewness Skewness skewness0.069
Kurtosis Kurtosis kurtosis-0.095
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha125800.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.274; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.996; Smooth: 0.991

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1rg6a_
Class classa — All alpha proteins
Fold Fold folda.60 — SAM domain-like
Superfamily Superfamily superfamilya.60.1 — SAM/Pointed domain
Family Family familya.60.1.2 — SAM (sterile alpha motif) domain

CATH v4.4 (1 domains)

Domain ID domain_id1rg6A00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology150 — DNA polymerase; domain 1
Homologous superfamily homologous superfamily50 — Transcription Factor, Ets-1

8. Citations (1)

9. Files and Curves (10)