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- PDB-2wtv: Aurora-A Inhibitor Structure -

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Basic information

Entry
Database: PDB / ID: 2wtv
TitleAurora-A Inhibitor Structure
ComponentsSERINE/THREONINE-PROTEIN KINASE 6 AURORA/IPL1-RELATED KINASE 1, BREAST TUMOR-AMPLIFIED KINASE, AURORA-A, AURORA-RELATED KINASE 1, HARK1
KeywordsTRANSFERASE / KINASE / CELL CYCLE / PHOSPHOPROTEIN
Function / homology
Function and homology information


Interaction between PHLDA1 and AURKA / regulation of centrosome cycle / axon hillock / spindle assembly involved in female meiosis I / cilium disassembly / spindle pole centrosome / histone H3S10 kinase activity / chromosome passenger complex / positive regulation of oocyte maturation / pronucleus ...Interaction between PHLDA1 and AURKA / regulation of centrosome cycle / axon hillock / spindle assembly involved in female meiosis I / cilium disassembly / spindle pole centrosome / histone H3S10 kinase activity / chromosome passenger complex / positive regulation of oocyte maturation / pronucleus / mitotic centrosome separation / meiotic spindle / germinal vesicle / protein localization to centrosome / anterior/posterior axis specification / centrosome localization / spindle organization / neuron projection extension / positive regulation of mitochondrial fission / mitotic spindle pole / SUMOylation of DNA replication proteins / spindle midzone / regulation of G2/M transition of mitotic cell cycle / protein serine/threonine/tyrosine kinase activity / centriole / AURKA Activation by TPX2 / positive regulation of mitotic nuclear division / positive regulation of mitotic cell cycle / mitotic spindle organization / TP53 Regulates Transcription of Genes Involved in G2 Cell Cycle Arrest / ciliary basal body / regulation of cytokinesis / regulation of signal transduction by p53 class mediator / negative regulation of protein binding / molecular function activator activity / liver regeneration / FBXL7 down-regulates AURKA during mitotic entry and in early mitosis / APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1 / regulation of protein stability / mitotic spindle / kinetochore / response to wounding / spindle / G2/M transition of mitotic cell cycle / microtubule cytoskeleton / Regulation of PLK1 Activity at G2/M Transition / positive regulation of proteasomal ubiquitin-dependent protein catabolic process / mitotic cell cycle / midbody / peptidyl-serine phosphorylation / basolateral plasma membrane / proteasome-mediated ubiquitin-dependent protein catabolic process / Regulation of TP53 Activity through Phosphorylation / protein autophosphorylation / microtubule / postsynaptic density / non-specific serine/threonine protein kinase / protein kinase activity / protein heterodimerization activity / protein phosphorylation / cell division / negative regulation of gene expression / protein serine kinase activity / protein serine/threonine kinase activity / centrosome / glutamatergic synapse / ubiquitin protein ligase binding / negative regulation of apoptotic process / apoptotic process / protein kinase binding / perinuclear region of cytoplasm / nucleoplasm / ATP binding / nucleus / cytosol
Similarity search - Function
Aurora kinase A / Aurora kinase / Transferase(Phosphotransferase) domain 1 / Transferase(Phosphotransferase); domain 1 / Phosphorylase Kinase; domain 1 / Phosphorylase Kinase; domain 1 / Serine/threonine-protein kinase, active site / Serine/Threonine protein kinases active-site signature. / Protein kinase domain / Serine/Threonine protein kinases, catalytic domain ...Aurora kinase A / Aurora kinase / Transferase(Phosphotransferase) domain 1 / Transferase(Phosphotransferase); domain 1 / Phosphorylase Kinase; domain 1 / Phosphorylase Kinase; domain 1 / Serine/threonine-protein kinase, active site / Serine/Threonine protein kinases active-site signature. / Protein kinase domain / Serine/Threonine protein kinases, catalytic domain / Protein kinase, ATP binding site / Protein kinases ATP-binding region signature. / Protein kinase domain profile. / Protein kinase domain / Protein kinase-like domain superfamily / 2-Layer Sandwich / Orthogonal Bundle / Mainly Alpha / Alpha Beta
Similarity search - Domain/homology
ACETATE ION / Chem-ZZL / Aurora kinase A
Similarity search - Component
Biological speciesHOMO SAPIENS (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.4 Å
AuthorsKosmopoulou, M. / Bayliss, R.
CitationJournal: Biochem.J. / Year: 2010
Title: Crystal Structure of an Aurora-A Mutant that Mimics Aurora-B Bound to Mln8054: Insights Into Selectivity and Drug Design.
Authors: Dodson, C.A. / Kosmopoulou, M. / Richards, M.W. / Atrash, B. / Bavetsias, V. / Blagg, J. / Bayliss, R.
History
DepositionSep 22, 2009Deposition site: PDBE / Processing site: PDBE
Revision 1.0Jan 26, 2010Provider: repository / Type: Initial release
Revision 1.1May 8, 2011Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Dec 20, 2023Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Other / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_database_status / pdbx_initial_refinement_model / struct_conn / struct_site
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.status_code_sf / _struct_conn.pdbx_leaving_atom_flag / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: SERINE/THREONINE-PROTEIN KINASE 6 AURORA/IPL1-RELATED KINASE 1, BREAST TUMOR-AMPLIFIED KINASE, AURORA-A, AURORA-RELATED KINASE 1, HARK1
B: SERINE/THREONINE-PROTEIN KINASE 6 AURORA/IPL1-RELATED KINASE 1, BREAST TUMOR-AMPLIFIED KINASE, AURORA-A, AURORA-RELATED KINASE 1, HARK1
C: SERINE/THREONINE-PROTEIN KINASE 6 AURORA/IPL1-RELATED KINASE 1, BREAST TUMOR-AMPLIFIED KINASE, AURORA-A, AURORA-RELATED KINASE 1, HARK1
D: SERINE/THREONINE-PROTEIN KINASE 6 AURORA/IPL1-RELATED KINASE 1, BREAST TUMOR-AMPLIFIED KINASE, AURORA-A, AURORA-RELATED KINASE 1, HARK1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)136,19330
Polymers132,9164
Non-polymers3,27826
Water13,385743
1
A: SERINE/THREONINE-PROTEIN KINASE 6 AURORA/IPL1-RELATED KINASE 1, BREAST TUMOR-AMPLIFIED KINASE, AURORA-A, AURORA-RELATED KINASE 1, HARK1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)33,9646
Polymers33,2291
Non-polymers7355
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
2
B: SERINE/THREONINE-PROTEIN KINASE 6 AURORA/IPL1-RELATED KINASE 1, BREAST TUMOR-AMPLIFIED KINASE, AURORA-A, AURORA-RELATED KINASE 1, HARK1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)34,33312
Polymers33,2291
Non-polymers1,10511
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
3
C: SERINE/THREONINE-PROTEIN KINASE 6 AURORA/IPL1-RELATED KINASE 1, BREAST TUMOR-AMPLIFIED KINASE, AURORA-A, AURORA-RELATED KINASE 1, HARK1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)34,0107
Polymers33,2291
Non-polymers7816
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
4
D: SERINE/THREONINE-PROTEIN KINASE 6 AURORA/IPL1-RELATED KINASE 1, BREAST TUMOR-AMPLIFIED KINASE, AURORA-A, AURORA-RELATED KINASE 1, HARK1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)33,8865
Polymers33,2291
Non-polymers6574
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
Unit cell
Length a, b, c (Å)118.707, 118.707, 135.890
Angle α, β, γ (deg.)90.00, 90.00, 120.00
Int Tables number144
Space group name H-MP31

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Components

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Protein , 1 types, 4 molecules ABCD

#1: Protein
SERINE/THREONINE-PROTEIN KINASE 6 AURORA/IPL1-RELATED KINASE 1, BREAST TUMOR-AMPLIFIED KINASE, AURORA-A, AURORA-RELATED KINASE 1, HARK1


Mass: 33228.895 Da / Num. of mol.: 4 / Fragment: CATALYTIC DOMAIN, RESIDUES 122-403 / Mutation: YES
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) HOMO SAPIENS (human) / Plasmid: PET M11 / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3) / Variant (production host): CODONPLUS RPIL
References: UniProt: O14965, non-specific serine/threonine protein kinase

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Non-polymers , 5 types, 769 molecules

#2: Chemical
ChemComp-ZZL / 4-{[9-CHLORO-7-(2,6-DIFLUOROPHENYL)-5H-PYRIMIDO[5,4-D][2]BENZAZEPIN-2-YL]AMINO}BENZOIC ACID


Mass: 476.862 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C25H15ClF2N4O2
#3: Chemical
ChemComp-EDO / 1,2-ETHANEDIOL / ETHYLENE GLYCOL


Mass: 62.068 Da / Num. of mol.: 11 / Source method: obtained synthetically / Formula: C2H6O2
#4: Chemical
ChemComp-ACT / ACETATE ION


Mass: 59.044 Da / Num. of mol.: 9 / Source method: obtained synthetically / Formula: C2H3O2
#5: Chemical ChemComp-DMS / DIMETHYL SULFOXIDE


Mass: 78.133 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C2H6OS / Comment: DMSO, precipitant*YM
#6: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 743 / Source method: isolated from a natural source / Formula: H2O

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Details

Compound detailsENGINEERED RESIDUE IN CHAIN A, LEU 215 TO ARG ENGINEERED RESIDUE IN CHAIN A, THR 217 TO GLU ...ENGINEERED RESIDUE IN CHAIN A, LEU 215 TO ARG ENGINEERED RESIDUE IN CHAIN A, THR 217 TO GLU ENGINEERED RESIDUE IN CHAIN A, ARG 220 TO LYS ENGINEERED RESIDUE IN CHAIN B, LEU 215 TO ARG ENGINEERED RESIDUE IN CHAIN B, THR 217 TO GLU ENGINEERED RESIDUE IN CHAIN B, ARG 220 TO LYS ENGINEERED RESIDUE IN CHAIN C, LEU 215 TO ARG ENGINEERED RESIDUE IN CHAIN C, THR 217 TO GLU ENGINEERED RESIDUE IN CHAIN C, ARG 220 TO LYS ENGINEERED RESIDUE IN CHAIN D, LEU 215 TO ARG ENGINEERED RESIDUE IN CHAIN D, THR 217 TO GLU ENGINEERED RESIDUE IN CHAIN D, ARG 220 TO LYS

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION / Number of used crystals: 1

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Sample preparation

CrystalDensity Matthews: 4.2 Å3/Da / Density % sol: 70.7 % / Description: NONE
Crystal growDetails: 0.8M NAH2PO4 1.2M K2HPO4 0.1M NA ACETATE, PH 4.5

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: ESRF / Beamline: ID14-1 / Wavelength: 0.9334
DetectorType: ADSC CCD / Detector: CCD
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9334 Å / Relative weight: 1
ReflectionResolution: 2.4→59.3 Å / Num. obs: 83351 / % possible obs: 99.5 % / Observed criterion σ(I): 2 / Redundancy: 3.4 % / Biso Wilson estimate: 24.36 Å2 / Rmerge(I) obs: 0.08 / Net I/σ(I): 12.3
Reflection shellResolution: 2.4→2.53 Å / Redundancy: 2.7 % / Rmerge(I) obs: 0.35 / Mean I/σ(I) obs: 3.2 / % possible all: 97.6

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Processing

Software
NameVersionClassification
PHENIX(PHENIX.REFINE)refinement
MOSFLMdata reduction
SCALAdata scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB ENTRY 1OL7

1ol7


Resolution: 2.4→19.78 Å / SU ML: 0.3 / σ(F): 0.01 / Phase error: 21.78 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.211 3969 5 %
Rwork0.164 --
obs0.167 79206 94.7 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL / Bsol: 51.14 Å2 / ksol: 0.4 e/Å3
Displacement parameters
Baniso -1Baniso -2Baniso -3
1-5.6981 Å20 Å2-0 Å2
2--5.6981 Å20 Å2
3----11.3961 Å2
Refinement stepCycle: LAST / Resolution: 2.4→19.78 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms8671 0 224 743 9638
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0069127
X-RAY DIFFRACTIONf_angle_d1.04612330
X-RAY DIFFRACTIONf_dihedral_angle_d21.4673396
X-RAY DIFFRACTIONf_chiral_restr0.0661288
X-RAY DIFFRACTIONf_plane_restr0.0041555
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2.4001-2.42930.29931440.22352379X-RAY DIFFRACTION83
2.4293-2.460.33651190.23262378X-RAY DIFFRACTION85
2.46-2.49230.3181220.2272423X-RAY DIFFRACTION85
2.4923-2.52640.32671170.22832547X-RAY DIFFRACTION88
2.5264-2.56240.30021190.22472521X-RAY DIFFRACTION88
2.5624-2.60050.28621460.2142485X-RAY DIFFRACTION89
2.6005-2.64110.28111380.19922599X-RAY DIFFRACTION90
2.6411-2.68430.22921360.19892596X-RAY DIFFRACTION92
2.6843-2.73040.28451280.19632625X-RAY DIFFRACTION92
2.7304-2.780.25281490.2012674X-RAY DIFFRACTION94
2.78-2.83330.25771320.18462708X-RAY DIFFRACTION95
2.8333-2.89090.22941420.18562709X-RAY DIFFRACTION95
2.8909-2.95360.23921380.18632661X-RAY DIFFRACTION95
2.9536-3.02210.23951520.18262742X-RAY DIFFRACTION97
3.0221-3.09740.21961510.16732732X-RAY DIFFRACTION97
3.0974-3.18080.18681600.15782751X-RAY DIFFRACTION97
3.1808-3.2740.22161400.15522769X-RAY DIFFRACTION98
3.274-3.37920.21151380.1522828X-RAY DIFFRACTION98
3.3792-3.49930.19231550.14122769X-RAY DIFFRACTION98
3.4993-3.63860.17941510.13542779X-RAY DIFFRACTION99
3.6386-3.80310.15231630.12752837X-RAY DIFFRACTION99
3.8031-4.0020.17441460.1252812X-RAY DIFFRACTION99
4.002-4.25040.14731420.11442833X-RAY DIFFRACTION99
4.2504-4.57490.15051420.11522819X-RAY DIFFRACTION99
4.5749-5.02840.1441280.11882837X-RAY DIFFRACTION100
5.0284-5.74040.20171620.15212783X-RAY DIFFRACTION99
5.7404-7.17450.20381590.16432811X-RAY DIFFRACTION100
7.1745-19.78510.151500.15262830X-RAY DIFFRACTION99

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