7ccw

Crystal structure of death-associated protein kinase 1 in complex with resveratrol and MES

Method: X-RAY DIFFRACTION Dmax: 64.8 Å Quality: EXCELLENT

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

Death-associated protein kinase 1

Homo sapiens

UniProt P53355

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 1–285 Not recorded STL RESVERATROL × 1 MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID × 1 SO4 SULFATE ION × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;1.8 M ammonium sulfate, 0.1 M MES-NaOH pH 6.5, 14.4 mg/mL DAPK1, 2 mM resveratrol Resolution 1.40 Å R-free 0.188

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.

77 other PDB entries and 81 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name DAPK1_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–285; UniProt 1–285

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 7ccw

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id7ccw
Deposition date deposition_date2020-06-18
Structure title titleCrystal structure of death-associated protein kinase 1 in complex with resveratrol and MES
Keywords keywordsprotein kinase, inhibitor, complex, natural compound, TRANSFERASE; TRANSFERASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier20.72
Radius of gyration Rg (electron density) rg_electron19.34
Forward intensity I(0) i017577400.00
Molecular weight molecular_weight32366.0 kDa
Excluded volume excluded_volume40806 ų
Envelope volume envelope_volume47509 ų
Hydration-shell volume shell_volume20488 ų
Envelope diameter envelope_diameter65.9
Shell Rg shell_rg25.78
Envelope Rg envelope_rg19.62
Shape Rg shape_rg19.33
Total Rg total_rg20.28
Total atoms total_atoms2282
Residues n_residues276
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 dmax64.8
Rg (real space) rg_real20.65
Rg uncertainty (real space) rg_real_error0.37
I(0) (real space) i0_real1.7580e+07
I(0) uncertainty (real space) i0_real_error2.3430e+05
Rg (reciprocal space) rg_reciprocal20.67
I(0) (reciprocal space) i0_reciprocal17580000.0000
Solution quality estimate total_estimate0.9026
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary62.9
Skewness Skewness skewness0.259
Kurtosis Kurtosis kurtosis-0.366
Angular range angular_range— – 0.3850 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha4115000.0000
Real-space data points n_real_points70
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.912; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.998; Smooth: 0.995

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 1 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd7ccwa_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.144 — Protein kinase-like (PK-like)
Superfamily Superfamily superfamilyd.144.1 — Protein kinase-like (PK-like)
Family Family familyd.144.1.7 — Protein kinases, catalytic subunit

8. Citations (1)

9. Files and Curves (10)