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- PDB-6bh9: Caspase-3 Mutant - T152A -

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Basic information

Entry
Database: PDB / ID: 6bh9
TitleCaspase-3 Mutant - T152A
Components
  • (Caspase-3Caspase 3) x 2
  • Ac-Asp-Glu-Val-Asp-CMK
Keywordsapoptosis/inhibitor / allosteric regulation / apoptosis / biophysics / caspase / computational biology / X-ray crystallography / fluorescence / molecular dynamics / protein evolution / apoptosis-inhibitor complex
Function / homology
Function and homology information


caspase-3 / Stimulation of the cell death response by PAK-2p34 / phospholipase A2 activator activity / anterior neural tube closure / intrinsic apoptotic signaling pathway in response to osmotic stress / leukocyte apoptotic process / positive regulation of pyroptotic inflammatory response / glial cell apoptotic process / NADE modulates death signalling / luteolysis ...caspase-3 / Stimulation of the cell death response by PAK-2p34 / phospholipase A2 activator activity / anterior neural tube closure / intrinsic apoptotic signaling pathway in response to osmotic stress / leukocyte apoptotic process / positive regulation of pyroptotic inflammatory response / glial cell apoptotic process / NADE modulates death signalling / luteolysis / response to cobalt ion / cysteine-type endopeptidase activity involved in apoptotic signaling pathway / death-inducing signaling complex / cyclin-dependent protein serine/threonine kinase inhibitor activity / cellular response to staurosporine / Apoptosis induced DNA fragmentation / cysteine-type endopeptidase activity involved in execution phase of apoptosis / Caspase activation via Dependence Receptors in the absence of ligand / Apoptotic cleavage of cell adhesion proteins / death receptor binding / SMAC, XIAP-regulated apoptotic response / axonal fasciculation / Activation of caspases through apoptosome-mediated cleavage / Signaling by Hippo / SMAC (DIABLO) binds to IAPs / SMAC(DIABLO)-mediated dissociation of IAP:caspase complexes / cysteine-type endopeptidase activity involved in apoptotic process / fibroblast apoptotic process / execution phase of apoptosis / negative regulation of cytokine production / epithelial cell apoptotic process / platelet formation / Other interleukin signaling / positive regulation of amyloid-beta formation / Apoptotic cleavage of cellular proteins / negative regulation of B cell proliferation / pyroptotic inflammatory response / T cell homeostasis / negative regulation of activated T cell proliferation / neurotrophin TRK receptor signaling pathway / B cell homeostasis / protein maturation / negative regulation of cell cycle / response to X-ray / regulation of macroautophagy / Caspase-mediated cleavage of cytoskeletal proteins / cell fate commitment / response to amino acid / Pyroptosis / response to tumor necrosis factor / enzyme activator activity / response to glucose / response to UV / response to glucocorticoid / keratinocyte differentiation / striated muscle cell differentiation / Degradation of the extracellular matrix / intrinsic apoptotic signaling pathway / erythrocyte differentiation / hippocampus development / apoptotic signaling pathway / sensory perception of sound / response to nicotine / protein catabolic process / regulation of protein stability / neuron differentiation / response to hydrogen peroxide / protein processing / response to wounding / positive regulation of neuron apoptotic process / response to estradiol / heart development / peptidase activity / neuron apoptotic process / protease binding / response to lipopolysaccharide / aspartic-type endopeptidase activity / learning or memory / response to hypoxia / response to xenobiotic stimulus / cysteine-type endopeptidase activity / neuronal cell body / apoptotic process / DNA damage response / protein-containing complex binding / proteolysis / nucleoplasm / nucleus / cytosol / cytoplasm
Similarity search - Function
Caspase-like / Rossmann fold - #1460 / Peptidase family C14A, His active site / Caspase family histidine active site. / Peptidase C14, caspase non-catalytic subunit p10 / Peptidase family C14A, cysteine active site / Caspase family cysteine active site. / Caspase family p10 domain profile. / Peptidase C14A, caspase catalytic domain / Caspase, interleukin-1 beta converting enzyme (ICE) homologues ...Caspase-like / Rossmann fold - #1460 / Peptidase family C14A, His active site / Caspase family histidine active site. / Peptidase C14, caspase non-catalytic subunit p10 / Peptidase family C14A, cysteine active site / Caspase family cysteine active site. / Caspase family p10 domain profile. / Peptidase C14A, caspase catalytic domain / Caspase, interleukin-1 beta converting enzyme (ICE) homologues / Peptidase C14, p20 domain / Caspase family p20 domain profile. / : / Caspase domain / Caspase-like domain superfamily / Alpha-Beta Plaits / Rossmann fold / 2-Layer Sandwich / 3-Layer(aba) Sandwich / Alpha Beta
Similarity search - Domain/homology
Ac-Asp-Glu-Val-Asp-CMK / Caspase-3
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / Resolution: 1.94 Å
AuthorsThomas, M.E. / Grinshpon, R. / Swartz, P.D. / Clark, A.C.
CitationJournal: J. Biol. Chem. / Year: 2018
Title: Modifications to a common phosphorylation network provide individualized control in caspases.
Authors: Thomas, M.E. / Grinshpon, R. / Swartz, P. / Clark, A.C.
History
DepositionOct 30, 2017Deposition site: RCSB / Processing site: RCSB
Revision 1.0Feb 21, 2018Provider: repository / Type: Initial release
Revision 1.1Apr 25, 2018Group: Data collection / Database references / Category: citation
Item: _citation.journal_volume / _citation.page_first / _citation.page_last

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Caspase-3
C: Caspase-3
B: Caspase-3
E: Caspase-3
D: Ac-Asp-Glu-Val-Asp-CMK
G: Ac-Asp-Glu-Val-Asp-CMK
hetero molecules


Theoretical massNumber of molelcules
Total (without water)64,76213
Polymers64,5766
Non-polymers1867
Water7,837435
1
A: Caspase-3
C: Caspase-3
G: Ac-Asp-Glu-Val-Asp-CMK
hetero molecules


Theoretical massNumber of molelcules
Total (without water)32,3927
Polymers32,2883
Non-polymers1044
Water543
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area6040 Å2
ΔGint-78 kcal/mol
Surface area11680 Å2
MethodPISA
2
B: Caspase-3
E: Caspase-3
D: Ac-Asp-Glu-Val-Asp-CMK
hetero molecules


Theoretical massNumber of molelcules
Total (without water)32,3696
Polymers32,2883
Non-polymers813
Water543
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area5880 Å2
ΔGint-65 kcal/mol
Surface area11660 Å2
MethodPISA
Unit cell
Length a, b, c (Å)108.362, 96.077, 68.212
Angle α, β, γ (deg.)90.00, 128.96, 90.00
Int Tables number5
Space group name H-MC121

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Components

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Protein , 2 types, 4 molecules ABCE

#1: Protein Caspase-3 / Caspase 3 / CASP-3 / Apopain / Cysteine protease CPP32 / CPP-32 / Protein Yama / SREBP cleavage activity 1 / SCA-1


Mass: 19729.318 Da / Num. of mol.: 2 / Mutation: T152A
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: CASP3, CPP32 / Production host: Escherichia coli K-12 (bacteria) / References: UniProt: P42574, caspase-3
#2: Protein Caspase-3 / Caspase 3 / CASP-3 / Apopain / Cysteine protease CPP32 / CPP-32 / Protein Yama / SREBP cleavage activity 1 / SCA-1


Mass: 12023.761 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: CASP3, CPP32 / Production host: Escherichia coli K-12 (bacteria) / References: UniProt: P42574, caspase-3

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Protein/peptide , 1 types, 2 molecules DG

#3: Protein/peptide Ac-Asp-Glu-Val-Asp-CMK


Type: Peptide-like / Class: Inhibitor / Mass: 534.946 Da / Num. of mol.: 2 / Source method: obtained synthetically / Source: (synth.) Homo sapiens (human) / References: Ac-Asp-Glu-Val-Asp-CMK

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Non-polymers , 3 types, 442 molecules

#4: Chemical
ChemComp-NA / SODIUM ION


Mass: 22.990 Da / Num. of mol.: 5 / Source method: obtained synthetically / Formula: Na
#5: Chemical ChemComp-CL / CHLORIDE ION / Chloride


Mass: 35.453 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Cl
#6: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 435 / Source method: isolated from a natural source / Formula: H2O

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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: 2.14 Å3/Da / Density % sol: 42.5 %
Crystal growTemperature: 291 K / Method: vapor diffusion, hanging drop
Details: Crystals were obtained at 18 C by the hanging drop vapor diffusion method using 4 mL drops that contained equal volumes of protein and reservoir solutions over a 0.5 mL solution of 100 mM ...Details: Crystals were obtained at 18 C by the hanging drop vapor diffusion method using 4 mL drops that contained equal volumes of protein and reservoir solutions over a 0.5 mL solution of 100 mM sodium citrate, pH 4.9-5.2, 8-18 % PEG 6000 (w/v), 10 mM DTT, and 3 mM NaN3. Crystals appeared within 3-5 days and were briefly immersed in a cryogenic solution containing 10% MPD (2-methylpentane-2,4-diol) and 90% reservoir solution.

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 22-BM / Wavelength: 1 Å
DetectorType: MAR scanner 300 mm plate / Detector: IMAGE PLATE / Date: Oct 21, 2013
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 1.94→50 Å / Num. obs: 40012 / % possible obs: 99.5 % / Redundancy: 2.9 % / Net I/σ(I): 14

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Processing

Software
NameVersionClassification
PHENIX(1.12_2829: ???)refinement
HKL-2000data reduction
HKL-2000data scaling
PHENIXphasing
RefinementResolution: 1.94→35.606 Å / SU ML: 0.17 / Cross valid method: FREE R-VALUE / σ(F): 1.34 / Phase error: 16.85 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.1887 2005 5.01 %
Rwork0.1457 --
obs0.1477 40012 99.51 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Refinement stepCycle: LAST / Resolution: 1.94→35.606 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms3907 0 7 435 4349
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0064106
X-RAY DIFFRACTIONf_angle_d0.8785540
X-RAY DIFFRACTIONf_dihedral_angle_d4.9114217
X-RAY DIFFRACTIONf_chiral_restr0.055601
X-RAY DIFFRACTIONf_plane_restr0.005716
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
1.9399-1.98840.1851390.15352598X-RAY DIFFRACTION97
1.9884-2.04220.21961400.15432727X-RAY DIFFRACTION99
2.0422-2.10230.18911400.14772686X-RAY DIFFRACTION99
2.1023-2.17010.20751430.1532723X-RAY DIFFRACTION100
2.1701-2.24770.20981410.13922686X-RAY DIFFRACTION100
2.2477-2.33770.19671470.14382743X-RAY DIFFRACTION100
2.3377-2.4440.16791400.14062685X-RAY DIFFRACTION100
2.444-2.57280.22651460.15342740X-RAY DIFFRACTION100
2.5728-2.7340.18971440.15762714X-RAY DIFFRACTION100
2.734-2.9450.21851450.15842713X-RAY DIFFRACTION100
2.945-3.24120.2091430.15622737X-RAY DIFFRACTION100
3.2412-3.70970.1761420.1372719X-RAY DIFFRACTION100
3.7097-4.67220.13871480.11742756X-RAY DIFFRACTION100
4.6722-35.61240.18481470.15732780X-RAY DIFFRACTION100

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