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- PDB-2c3l: Identification of a buried pocket for potent and selective inhibi... -

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Basic information

Entry
Database: PDB / ID: 2c3l
TitleIdentification of a buried pocket for potent and selective inhibition of Chk1: prediction and verification
ComponentsSERINE/THREONINE-PROTEIN KINASE CHK1
KeywordsTRANSFERASE / DRUG DESIGN / MOLECULAR MODELING / MOLECULAR RECOGNITION / ONCOLOGY / ATP-BINDING / CELL CYCLE / DNA DAMAGE / DNA REPAIR / KINASE / NUCLEAR PROTEIN / NUCLEOTIDE-BINDING / PHOSPHORYLATION / POLYMORPHISM / SERINE/THREONINE-PROTEIN KINASE / UBL CONJUGATION
Function / homology
Function and homology information


regulation of transcription from RNA polymerase II promoter in response to UV-induced DNA damage / histone kinase activity (H3-T11 specific) / negative regulation of mitotic nuclear division / regulation of histone H3-K9 acetylation / chromatin-mediated maintenance of transcription / regulation of mitotic centrosome separation / signal transduction involved in G2 DNA damage checkpoint / regulation of double-strand break repair via homologous recombination / DNA damage induced protein phosphorylation / negative regulation of G0 to G1 transition ...regulation of transcription from RNA polymerase II promoter in response to UV-induced DNA damage / histone kinase activity (H3-T11 specific) / negative regulation of mitotic nuclear division / regulation of histone H3-K9 acetylation / chromatin-mediated maintenance of transcription / regulation of mitotic centrosome separation / signal transduction involved in G2 DNA damage checkpoint / regulation of double-strand break repair via homologous recombination / DNA damage induced protein phosphorylation / negative regulation of G0 to G1 transition / replicative senescence / positive regulation of cell cycle / condensed nuclear chromosome / DNA damage checkpoint / chromatin / cellular response to mechanical stimulus / peptidyl-threonine phosphorylation / kinase activity / regulation of signal transduction by p53 class mediator / DNA replication / non-specific serine/threonine protein kinase / intracellular signal transduction / cell cycle / protein kinase activity / centrosome / DNA repair / intracellular membrane-bounded organelle / protein domain specific binding / cellular response to DNA damage stimulus / apoptotic process / protein serine/threonine kinase activity / protein phosphorylation / protein-containing complex / extracellular space / nucleoplasm / ATP binding / nucleus / cytosol / cytoplasm
Serine/threonine-protein kinase, active site / Protein kinase domain / Protein kinase domain / Checkpoint kinase 1, catalytic domain / Protein kinase, ATP binding site / Protein kinase-like domain superfamily / Transferase(Phosphotransferase) domain 1 / Transferase(Phosphotransferase); domain 1 / Phosphorylase Kinase; domain 1 / Phosphorylase Kinase; domain 1 ...Serine/threonine-protein kinase, active site / Protein kinase domain / Protein kinase domain / Checkpoint kinase 1, catalytic domain / Protein kinase, ATP binding site / Protein kinase-like domain superfamily / Transferase(Phosphotransferase) domain 1 / Transferase(Phosphotransferase); domain 1 / Phosphorylase Kinase; domain 1 / Phosphorylase Kinase; domain 1 / 2-Layer Sandwich / Orthogonal Bundle / Mainly Alpha / Alpha Beta
Serine/threonine-protein kinase Chk1
Biological speciesHOMO SAPIENS (human)
MethodX-RAY DIFFRACTION / MOLECULAR REPLACEMENT / Resolution: 2.35 Å
AuthorsFoloppe, N. / Fisher, L.M. / Francis, G. / Howes, R. / Kierstan, P. / Potter, A.
CitationJournal: Bioorg.Med.Chem. / Year: 2006
Title: Identification of a Buried Pocket for Potent and Selective Inhibition of Chk1: Prediction and Verification.
Authors: Foloppe, N. / Fisher, L.M. / Francis, G. / Howes, R. / Kierstan, P. / Potter, A.
Validation Report
SummaryFull reportAbout validation report
History
DepositionOct 10, 2005Deposition site: PDBE / Processing site: PDBE
Revision 1.0Nov 23, 2005Provider: repository / Type: Initial release
Revision 1.1May 7, 2011Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Jul 12, 2017Group: Data collection / Category: diffrn_source / Item: _diffrn_source.type

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: SERINE/THREONINE-PROTEIN KINASE CHK1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)34,4783
Polymers34,1481
Non-polymers3302
Water4,197233
1


TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPQS
Unit cell
γ
α
β
Length a, b, c (Å)44.980, 65.862, 58.086
Angle α, β, γ (deg.)90.00, 94.63, 90.00
Int Tables number4
Space group name H-MP1211

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Components

#1: Protein SERINE/THREONINE-PROTEIN KINASE CHK1 / CHK1 KINASE


Mass: 34148.148 Da / Num. of mol.: 1 / Fragment: N-TERMINAL KINASE DOMAIN, RESIDUES 1-289
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) HOMO SAPIENS (human) / Plasmid: PFASTBAC1/CHK1 1-289 C8H / Cell line (production host): SF9 / Production host: SPODOPTERA FRUGIPERDA (fall armyworm) / References: UniProt: O14757, EC: 2.7.1.37
#2: Chemical ChemComp-IDZ / 3-(1H-BENZIMIDAZOL-2-YL)-1H-INDAZOLE


Mass: 234.256 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C14H10N4
#3: Chemical ChemComp-SO4 / SULFATE ION / Sulfate


Mass: 96.063 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: SO4
#4: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 233 / Source method: isolated from a natural source / Formula: H2O
Compound detailsINVOLED IN THE PROCESS OF RESPONSE TO DNA DAMAGE OR THE PRESENCE OF UNREPLICATED DNA.

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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: 2.55 Å3/Da / Density % sol: 51.47 %
Crystal growpH: 7.5 / Details: pH 7.50

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: ROTATING ANODE / Type: RIGAKU RUH3R / Wavelength: 1.5418
DetectorType: RIGAKU RAXIS IV / Detector: IMAGE PLATE / Date: Jun 26, 2003 / Details: BLUE OSMIC MIRRORS
RadiationMonochromator: CU FILTER / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.5418 Å / Relative weight: 1
ReflectionResolution: 2.35→30 Å / Num. obs: 14217 / % possible obs: 95.1 % / Observed criterion σ(I): 2 / Redundancy: 2 % / Rmerge(I) obs: 0.09 / Net I/σ(I): 9.6
Reflection shellResolution: 2.35→2.41 Å / Redundancy: 1 % / Rmerge(I) obs: 0.35 / Mean I/σ(I) obs: 3.7 / % possible all: 82.9

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Processing

Software
NameVersionClassification
REFMAC5.1.09refinement
d*TREKdata reduction
d*TREKdata scaling
AMoREphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB ENTRY 1IA8

1ia8


Resolution: 2.35→65.94 Å / Cor.coef. Fo:Fc: 0.95 / Cor.coef. Fo:Fc free: 0.89 / SU B: 8.495 / SU ML: 0.199 / Cross valid method: THROUGHOUT / ESU R: 0.384 / ESU R Free: 0.292 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS.
RfactorNum. reflection% reflectionSelection details
Rfree0.279 672 5 %RANDOM
Rwork0.185 ---
Obs0.189 12875 95.3 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: BABINET MODEL WITH MASK
Displacement parametersBiso mean: 45.92 Å2
Baniso -1Baniso -2Baniso -3
1--1.27 Å20 Å2-1.07 Å2
2--0.44 Å20 Å2
3---0.65 Å2
Refinement stepCycle: LAST / Resolution: 2.35→65.94 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms2142 0 23 233 2398
Refine LS restraints
Refinement-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0250.0212218
X-RAY DIFFRACTIONr_bond_other_d
X-RAY DIFFRACTIONr_angle_refined_deg2.2891.9713006
X-RAY DIFFRACTIONr_angle_other_deg
X-RAY DIFFRACTIONr_dihedral_angle_1_deg7.8055263
X-RAY DIFFRACTIONr_dihedral_angle_2_deg
X-RAY DIFFRACTIONr_dihedral_angle_3_deg24.03315390
X-RAY DIFFRACTIONr_dihedral_angle_4_deg21.0931514
X-RAY DIFFRACTIONr_chiral_restr0.1770.2321
X-RAY DIFFRACTIONr_gen_planes_refined0.0090.021683
X-RAY DIFFRACTIONr_gen_planes_other
X-RAY DIFFRACTIONr_nbd_refined0.2470.21074
X-RAY DIFFRACTIONr_nbd_other
X-RAY DIFFRACTIONr_nbtor_refined
X-RAY DIFFRACTIONr_nbtor_other
X-RAY DIFFRACTIONr_xyhbond_nbd_refined0.2170.2195
X-RAY DIFFRACTIONr_xyhbond_nbd_other
X-RAY DIFFRACTIONr_metal_ion_refined
X-RAY DIFFRACTIONr_metal_ion_other
X-RAY DIFFRACTIONr_symmetry_vdw_refined0.3350.264
X-RAY DIFFRACTIONr_symmetry_vdw_other
X-RAY DIFFRACTIONr_symmetry_hbond_refined0.4720.221
X-RAY DIFFRACTIONr_symmetry_hbond_other
X-RAY DIFFRACTIONr_symmetry_metal_ion_refined
X-RAY DIFFRACTIONr_symmetry_metal_ion_other
X-RAY DIFFRACTIONr_mcbond_it1.2791.51322
X-RAY DIFFRACTIONr_mcbond_other
X-RAY DIFFRACTIONr_mcangle_it2.26622137
X-RAY DIFFRACTIONr_mcangle_other
X-RAY DIFFRACTIONr_scbond_it3.5933896
X-RAY DIFFRACTIONr_scbond_other
X-RAY DIFFRACTIONr_scangle_it5.414.5869
X-RAY DIFFRACTIONr_scangle_other
X-RAY DIFFRACTIONr_long_range_B_refined
X-RAY DIFFRACTIONr_long_range_B_other
X-RAY DIFFRACTIONr_rigid_bond_restr
X-RAY DIFFRACTIONr_sphericity_free
X-RAY DIFFRACTIONr_sphericity_bonded
LS refinement shellResolution: 2.35→2.41 Å / Total num. of bins used: 20 /
RfactorNum. reflection
Rfree0.382 59
Rwork0.241 943

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