3DJ5

Crystal structure of the mouse Aurora-A catalytic domain (Asn186->Gly, Lys240->Arg, Met302->Leu) in complex with Compound 290.

PDB DOI: https://doi.org/10.2210/pdb3DJ5/pdb

Classification: TRANSFERASE
Organism(s): Mus musculus
Expression System: Escherichia coli
Mutation(s): Yes

Deposited: 2008-06-22 Released: 2009-05-05
Deposition Author(s): Elling, R.A., Erlanson, D.A., Yang, W., Tangonan, B.T., Hansen, S.K., Romanowski, M.J.

Experimental Data Snapshot

Method: X-RAY DIFFRACTION
Resolution: 1.80 Å
R-Value Free: 0.243
R-Value Work: 0.207
R-Value Observed: 0.210

wwPDB Validation 3D Report Full Report

Ligand Structure Quality Assessment

This is version 1.4 of the entry. See complete history.

Literature

New fragment-based drug discovery

Elling, R.A., A Erlanson, D., Yang, W., Tangonan, B.T., Hansen, S.K., Romanowski, M.J.

To be published.

Macromolecule Content

Total Structure Weight: 32.05 kDa
Atom Count: 2,477
Modelled Residue Count: 252
Deposited Residue Count: 272
Unique protein chains: 1

Macromolecules

Find similar proteins by:

(by identity cutoff) | 3D Structure

Entity ID: 1
Molecule	Chains	Sequence Length	Organism	Details	Image
serine/threonine kinase 6	A	272	Mus musculus	Mutation(s): 3 Gene Names: Aurka, Stk6 EC: 2.7.11.1
UniProt & NIH Common Fund Data Resources
Find proteins for P97477 (Mus musculus) Explore P97477 Go to UniProtKB: P97477
IMPC: MGI:894678
Entity Groups
Sequence Clusters	30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt Group	P97477
Sequence Annotations Expand
Reference Sequence

Small Molecules

Ligands 1 Unique
ID	Chains	Name / Formula / InChI Key	2D Diagram	3D Interactions
AK5 Query on AK5 Download Ideal Coordinates CCD File SDF format, chain B [auth A] MOL2 format, chain B [auth A]	B [auth A]	3-({3-[(6-amino-5-bromopyrimidin-4-yl)sulfanyl]propanoyl}amino)-4-methoxy-N-phenylbenzamide C₂₁ H₂₀ Br N₅ O₃ S SSEJHILVXYLIBN-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: 1.80 Å
R-Value Free: 0.243
R-Value Work: 0.207
R-Value Observed: 0.210
Space Group: P 3₂ 2 1

Unit Cell:

Length ( Å )	Angle ( ˚ )
a = 97.738	α = 90
b = 97.738	β = 90
c = 62.224	γ = 120

Software Package:

Software Name	Purpose
REFMAC	refinement
ADSC	data collection
CrystalClear	data reduction
d*TREK	data scaling
MOLREP	phasing

Structure Validation

View Full Validation Report

Ligand Structure Quality Assessment

Entry History

Deposition Data

Released Date: 2009-05-05

Deposition Author(s):

Romanowski, M.J.

Revision History (Full details and data files)

Version 1.0: 2009-05-05
Type: Initial release
Version 1.1: 2011-07-13
Changes: Version format compliance
Version 1.2: 2018-01-24
Changes: Structure summary
Version 1.3: 2021-10-20
Changes: Database references, Derived calculations
Version 1.4: 2023-08-30
Changes: Data collection, Refinement description

RCSB PDB Core Operations are funded by the National Science Foundation (DBI-1832184), the US Department of Energy (DE-SC0019749), and the National Cancer Institute, National Institute of Allergy and Infectious Diseases, and National Institute of General Medical Sciences of the National Institutes of Health under grant R01GM133198.