3zxt

Dimeric structure of DAPK-1 catalytic domain in complex with AMPPCP- Mg

Method: X-RAY DIFFRACTION Dmax: 149.3 Å Quality: GOOD

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 homooligomer Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 1–285 Chain B; UniProt 1–285 Fragment:CATALYTIC DOMAIN, RESIDUES 1-285 ACP PHOSPHOMETHYLPHOSPHONIC ACID ADENYLATE ESTER × 2 MG MAGNESIUM ION × 4 X-RAY DIFFRACTION X-ray crystallization conditions:0.1 M HEPES PH7.0, 0.1M MGCL2, 15% PEG4000 Resolution 2.65 Å R-free 0.285
2 Protein homooligomer Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 1–285 Chain D; UniProt 1–285 Fragment:CATALYTIC DOMAIN, RESIDUES 1-285 ACP PHOSPHOMETHYLPHOSPHONIC ACID ADENYLATE ESTER × 2 MG MAGNESIUM ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:0.1 M HEPES PH7.0, 0.1M MGCL2, 15% PEG4000 Resolution 2.65 Å R-free 0.285

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 80 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 Author chain B; PDBConstruct 1–285; UniProt 1–285 Author chain C; PDBConstruct 1–285; UniProt 1–285 Author chain D; 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 3zxt

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3zxt
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2. Structure Basics 2. Structure Basics

Entry ID entry_id3zxt
Deposition date deposition_date2011-08-15
Structure title titleDimeric structure of DAPK-1 catalytic domain in complex with AMPPCP- Mg
Keywords keywordsAPOPTOSIS, TRANSFERASE, ATP BINDING; TRANSFERASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier42.81
Radius of gyration Rg (electron density) rg_electron42.76
Forward intensity I(0) i0179654000.00
Molecular weight molecular_weight110530.0 kDa
Excluded volume excluded_volume138740 ų
Envelope volume envelope_volume202210 ų
Hydration-shell volume shell_volume42309 ų
Envelope diameter envelope_diameter149.6
Shell Rg shell_rg44.09
Envelope Rg envelope_rg41.61
Shape Rg shape_rg42.78
Total Rg total_rg42.78
Total atoms total_atoms7804
Residues n_residues1006
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 dmax149.3
Rg (real space) rg_real43.06
Rg uncertainty (real space) rg_real_error1.71
I(0) (real space) i0_real1.7970e+08
I(0) uncertainty (real space) i0_real_error3.4330e+06
Rg (reciprocal space) rg_reciprocal42.82
I(0) (reciprocal space) i0_reciprocal179600000.0000
Solution quality estimate total_estimate0.8555
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary52.4
Skewness Skewness skewness0.411
Kurtosis Kurtosis kurtosis-0.442
Angular range angular_range— – 0.1850 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha11010000.0000
Real-space data points n_real_points38
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.807; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.857; Smooth: 0.838

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 12 domains

SCOP 2.08 (4 domains)

Domain ID domain_idd3zxta_
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
Domain ID domain_idd3zxtb_
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
Domain ID domain_idd3zxtc_
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
Domain ID domain_idd3zxtd_
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

CATH v4.4 (8 domains)

Domain ID domain_id3zxtA01
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology200 — Phosphorylase Kinase; domain 1
Homologous superfamily homologous superfamily20 — Phosphorylase Kinase; domain 1
Domain ID domain_id3zxtA02
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology510 — Transferase(Phosphotransferase); domain 1
Homologous superfamily homologous superfamily10 — Transferase(Phosphotransferase) domain 1
Domain ID domain_id3zxtB01
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology200 — Phosphorylase Kinase; domain 1
Homologous superfamily homologous superfamily20 — Phosphorylase Kinase; domain 1
Domain ID domain_id3zxtB02
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology510 — Transferase(Phosphotransferase); domain 1
Homologous superfamily homologous superfamily10 — Transferase(Phosphotransferase) domain 1
Domain ID domain_id3zxtC01
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology200 — Phosphorylase Kinase; domain 1
Homologous superfamily homologous superfamily20 — Phosphorylase Kinase; domain 1
Domain ID domain_id3zxtC02
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology510 — Transferase(Phosphotransferase); domain 1
Homologous superfamily homologous superfamily10 — Transferase(Phosphotransferase) domain 1
Domain ID domain_id3zxtD01
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology200 — Phosphorylase Kinase; domain 1
Homologous superfamily homologous superfamily20 — Phosphorylase Kinase; domain 1
Domain ID domain_id3zxtD02
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology510 — Transferase(Phosphotransferase); domain 1
Homologous superfamily homologous superfamily10 — Transferase(Phosphotransferase) domain 1

8. Citations (1)

9. Files and Curves (10)