2Y0A

Structure of DAPK1 construct residues 1-304

PDB DOI: https://doi.org/10.2210/pdb2Y0A/pdb

Classification: TRANSFERASE
Organism(s): Homo sapiens
Expression System: Escherichia coli BL21(DE3)
Mutation(s): No

Deposited: 2010-12-01 Released: 2011-12-14
Deposition Author(s): Yumerefendi, H., Mas, P.J., Dordevic, N., McCarthy, A.A., Hart, D.J.

Experimental Data Snapshot

Method: X-RAY DIFFRACTION
Resolution: 2.60 Å
R-Value Free: 0.259
R-Value Work: 0.200
R-Value Observed: 0.203

Starting Model: experimental
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wwPDB Validation 3D Report Full Report

This is version 1.1 of the entry. See complete history.

Literature

Library-Based Construct Screening of Death-Associated Protein Kinase 1 Identifies the Minimal Calmodulin Interaction Region and Autoinhibitory Conformation of the Catalytic Domain

Yumerefendi, H., Mas, P.J., Dordevic, N., Mccarthy, A.A., Hart, D.J.

To be published.

Macromolecule Content

Total Structure Weight: 37.46 kDa
Atom Count: 2,439
Modelled Residue Count: 300
Deposited Residue Count: 326
Unique protein chains: 1

Macromolecules

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(by identity cutoff) | 3D Structure

Entity ID: 1
Molecule	Chains	Sequence Length	Organism	Details	Image
DEATH-ASSOCIATED PROTEIN KINASE 1	A	326	Homo sapiens	Mutation(s): 0 EC: 2.7.11.1
UniProt & NIH Common Fund Data Resources
Find proteins for P53355 (Homo sapiens) Explore P53355 Go to UniProtKB: P53355
PHAROS: P53355 GTEx: ENSG00000196730
Entity Groups
Sequence Clusters	30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt Group	P53355
Sequence Annotations Expand
Reference Sequence

Small Molecules

Ligands 1 Unique
ID	Chains	Name / Formula / InChI Key	2D Diagram	3D Interactions
MES Query on MES Download Ideal Coordinates CCD File SDF format, chain B [auth A] MOL2 format, chain B [auth A] mmCIF format, chain B [auth A]	B [auth A]	2-(N-MORPHOLINO)-ETHANESULFONIC ACID C₆ H₁₃ N O₄ S SXGZJKUKBWWHRA-UHFFFAOYSA-N		Interactions Focus chain B [auth A] Interactions & Density Focus chain B [auth A]

Experimental Data & Validation

Experimental Data

Method: X-RAY DIFFRACTION
Resolution: 2.60 Å
R-Value Free: 0.259
R-Value Work: 0.200
R-Value Observed: 0.203
Space Group: P 2₁ 2₁ 2₁

Unit Cell:

Length ( Å )	Angle ( ˚ )
a = 50.22	α = 90
b = 78.88	β = 90
c = 111.47	γ = 90

Software Package:

Software Name	Purpose
REFMAC	refinement
MOSFLM	data reduction
SCALA	data scaling
PHASER	phasing

Structure Validation

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Entry History

Deposition Data

Released Date: 2011-12-14

Deposition Author(s):

Revision History (Full details and data files)

Version 1.0: 2011-12-14
Type: Initial release
Version 1.1: 2023-12-20
Changes: Data collection, Database references, Derived calculations, Other, Refinement description

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Help and Resources

2Y0A

Structure of DAPK1 construct residues 1-304

Library-Based Construct Screening of Death-Associated Protein Kinase 1 Identifies the Minimal Calmodulin Interaction Region and Autoinhibitory Conformation of the Catalytic Domain

Entity ID: 1

UniProt & NIH Common Fund Data Resources

Entity Groups

Sequence Annotations

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Experimental Data

Structure Validation

Deposition Data

Revision History (Full details and data files)