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- PDB-7h6e: THE 2.0 A CRYSTAL STRUCTURE OF HUMAN CHYMASE IN COMPLEX WITH 5-fl... -

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Basic information

Entry
Database: PDB / ID: 7h6e
TitleTHE 2.0 A CRYSTAL STRUCTURE OF HUMAN CHYMASE IN COMPLEX WITH 5-fluoro-3-methyl-N-(2-methylsulfonyl-4-pyridin-4-ylphenyl)-1-benzothiophene-2-sulfonamide
ComponentsChymase
KeywordsHYDROLASE / HUMAN CHYMASE / SERINE PROTEINASE
Function / homology
Function and homology information


chymase / basement membrane disassembly / cytokine precursor processing / peptide metabolic process / midbrain development / Activation of Matrix Metalloproteinases / extracellular matrix disassembly / Metabolism of Angiotensinogen to Angiotensins / angiotensin maturation / serine-type peptidase activity ...chymase / basement membrane disassembly / cytokine precursor processing / peptide metabolic process / midbrain development / Activation of Matrix Metalloproteinases / extracellular matrix disassembly / Metabolism of Angiotensinogen to Angiotensins / angiotensin maturation / serine-type peptidase activity / protein maturation / peptide binding / secretory granule / protein catabolic process / cellular response to glucose stimulus / Signaling by SCF-KIT / cytoplasmic ribonucleoprotein granule / positive regulation of angiogenesis / regulation of inflammatory response / : / endopeptidase activity / serine-type endopeptidase activity / extracellular space / extracellular region / cytosol
Similarity search - Function
Serine proteases, trypsin family, histidine active site / Serine proteases, trypsin family, serine active site / Serine proteases, trypsin family, histidine active site. / Peptidase S1A, chymotrypsin family / Serine proteases, trypsin family, serine active site. / Serine proteases, trypsin domain profile. / Trypsin-like serine protease / Serine proteases, trypsin domain / Trypsin / Peptidase S1, PA clan, chymotrypsin-like fold / Peptidase S1, PA clan
Similarity search - Domain/homology
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / MOLECULAR REPLACEMENT / Resolution: 2 Å
AuthorsBanner, D.W. / Benz, J.M. / Schlatter, D. / Hilpert, H.
Funding support Switzerland, 1items
OrganizationGrant numberCountry
Not funded Switzerland
CitationJournal: To be published
Title: Crystal structures of human Chymase and Cathepsin G
Authors: Markus, R. / Tosstorff, A.
History
DepositionApr 19, 2024Deposition site: RCSB / Processing site: RCSB
Revision 1.0Mar 5, 2025Provider: repository / Type: Initial release

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: Chymase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)25,5753
Polymers25,0331
Non-polymers5422
Water3,585199
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)59.080, 59.140, 72.490
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number19
Space group name H-MP212121

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Components

#1: Protein Chymase / Alpha-chymase / Mast cell protease I


Mass: 25032.910 Da / Num. of mol.: 1 / Mutation: NO
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: CMA1, CYH, CYM / Production host: Escherichia coli (E. coli) / References: UniProt: P23946, chymase
#2: Chemical ChemComp-ZN / ZINC ION


Mass: 65.409 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: Zn
#3: Chemical ChemComp-A1AOP / 5-fluoro-N-[2-(methanesulfonyl)-4-(pyridin-4-yl)phenyl]-3-methyl-1-benzothiophene-2-sulfonamide


Mass: 476.564 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C21H17FN2O4S3 / Feature type: SUBJECT OF INVESTIGATION
#4: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 199 / Source method: isolated from a natural source / Formula: H2O
Has protein modificationY

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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: 2.6 Å3/Da / Density % sol: 52.74 %
Crystal growTemperature: 293 K / Method: microbatch / pH: 8.5
Details: Sample of human Chymase in 50 mM MES/NaOH pH 5.5, 150mM NaCl, 1mM TCEP, 10% Glycerol) at a concentration of 11mg/ml to 14mg/ml.Add [2-[(4-methylpyridin-2-yl)amino]-2-oxoethyl] 2- ...Details: Sample of human Chymase in 50 mM MES/NaOH pH 5.5, 150mM NaCl, 1mM TCEP, 10% Glycerol) at a concentration of 11mg/ml to 14mg/ml.Add [2-[(4-methylpyridin-2-yl)amino]-2-oxoethyl] 2-methylquinoline-4-carboxylate at 10x molar ratio. The compound helps to obtain crystals but is not visible in the structures. Add 0.5 mM ZnCl2. Add inhibitor, incubate for 16h on ice. Crystallize using microbatch setups with Al's oil (Hampton Research), with total drop size 1ul with 50% protein sample, using crystallization reagent of 0.1M Tris/HCl pH 8.5, 0.2M NaCl, 25% PEG 3350.

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: ROTATING ANODE / Type: BRUKER AXS MICROSTAR / Wavelength: 1.5418 Å
DetectorType: MAR scanner 345 mm plate / Detector: IMAGE PLATE / Date: Feb 8, 2006
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.5418 Å / Relative weight: 1
ReflectionResolution: 2→19.03 Å / Num. obs: 15954 / % possible obs: 89.9 % / Rmerge(I) obs: 0.06 / Rrim(I) all: 0.07 / Net I/σ(I): 16.7 / Num. measured all: 59477
Reflection shell

Diffraction-ID: 1

Resolution (Å)% possible obs (%)Rmerge(I) obsNum. measured obsNum. unique obsRrim(I) allNet I/σ(I) obs
2-2.1292.50.259975025960.3025.3
2.12-2.2669.60.203665717650.2366.54
2.26-2.4482.40.135770520410.1589.58
2.44-2.6795.20.11830622020.12911.6
2.67-2.98960.076754320030.08815.68
2.98-3.4396.80.047670717950.05523.02
3.43-4.1696.70.036557715150.04228.89
4.16-5.7697.90.026455912540.0338.66
5.76-19.0395.10.02526737830.0339.72

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Processing

Software
NameVersionClassification
REFMAC5.8.0425refinement
XSCALEdata scaling
XDSdata reduction
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT / Resolution: 2→19.03 Å / Cor.coef. Fo:Fc: 0.947 / Cor.coef. Fo:Fc free: 0.892 / SU B: 4.924 / SU ML: 0.132 / Cross valid method: THROUGHOUT / ESU R: 0.205 / ESU R Free: 0.199 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
RfactorNum. reflection% reflectionSelection details
Rfree0.26071 799 5 %RANDOM
Rwork0.18478 ---
obs0.1884 15163 89.95 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK
Displacement parametersBiso mean: 22.755 Å2
Baniso -1Baniso -2Baniso -3
1-2.07 Å20 Å20 Å2
2---0.32 Å20 Å2
3----1.75 Å2
Refinement stepCycle: LAST / Resolution: 2→19.03 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms1709 0 32 199 1940
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0110.0121837
X-RAY DIFFRACTIONr_bond_other_d0.0010.0161738
X-RAY DIFFRACTIONr_angle_refined_deg1.7871.682496
X-RAY DIFFRACTIONr_angle_other_deg0.5711.5714011
X-RAY DIFFRACTIONr_dihedral_angle_1_deg7.9865227
X-RAY DIFFRACTIONr_dihedral_angle_2_deg30.83120.6182
X-RAY DIFFRACTIONr_dihedral_angle_3_deg14.08414.92312
X-RAY DIFFRACTIONr_dihedral_angle_4_deg19.5561514
X-RAY DIFFRACTIONr_chiral_restr0.0820.2235
X-RAY DIFFRACTIONr_gen_planes_refined0.0110.022077
X-RAY DIFFRACTIONr_gen_planes_other0.0010.02419
X-RAY DIFFRACTIONr_nbd_refined
X-RAY DIFFRACTIONr_nbd_other
X-RAY DIFFRACTIONr_nbtor_refined
X-RAY DIFFRACTIONr_nbtor_other
X-RAY DIFFRACTIONr_xyhbond_nbd_refined
X-RAY DIFFRACTIONr_xyhbond_nbd_other
X-RAY DIFFRACTIONr_metal_ion_refined
X-RAY DIFFRACTIONr_metal_ion_other
X-RAY DIFFRACTIONr_symmetry_vdw_refined
X-RAY DIFFRACTIONr_symmetry_vdw_other
X-RAY DIFFRACTIONr_symmetry_hbond_refined
X-RAY DIFFRACTIONr_symmetry_hbond_other
X-RAY DIFFRACTIONr_symmetry_metal_ion_refined
X-RAY DIFFRACTIONr_symmetry_metal_ion_other
X-RAY DIFFRACTIONr_mcbond_it2.8872.339903
X-RAY DIFFRACTIONr_mcbond_other2.8882.337902
X-RAY DIFFRACTIONr_mcangle_it4.2344.1771131
X-RAY DIFFRACTIONr_mcangle_other4.2324.1781132
X-RAY DIFFRACTIONr_scbond_it2.8942.614934
X-RAY DIFFRACTIONr_scbond_other2.8822.622900
X-RAY DIFFRACTIONr_scangle_it
X-RAY DIFFRACTIONr_scangle_other4.4094.7181313
X-RAY DIFFRACTIONr_long_range_B_refined6.541252141
X-RAY DIFFRACTIONr_long_range_B_other6.41622.682034
X-RAY DIFFRACTIONr_rigid_bond_restr
X-RAY DIFFRACTIONr_sphericity_free
X-RAY DIFFRACTIONr_sphericity_bonded
LS refinement shellResolution: 2→2.051 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.388 47 -
Rwork0.316 1129 -
obs--91.88 %

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