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- PDB-7y0e: Crystal structure of TMPRSS2 in complex with Camostat -

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Basic information

Entry
Database: PDB / ID: 7y0e
TitleCrystal structure of TMPRSS2 in complex with Camostat
Components(Transmembrane protease serine 2 catalytic ...) x 2
KeywordsHYDROLASE / Inhibitor / Complex / Host / Antiviral / ANTIVIRAL PROTEIN
Function / homology
Function and homology information


transmembrane protease serine 2 / protein autoprocessing / Attachment and Entry / serine-type peptidase activity / viral translation / Induction of Cell-Cell Fusion / Attachment and Entry / positive regulation of viral entry into host cell / serine-type endopeptidase activity / proteolysis ...transmembrane protease serine 2 / protein autoprocessing / Attachment and Entry / serine-type peptidase activity / viral translation / Induction of Cell-Cell Fusion / Attachment and Entry / positive regulation of viral entry into host cell / serine-type endopeptidase activity / proteolysis / extracellular exosome / extracellular region / nucleoplasm / plasma membrane
Similarity search - Function
Scavenger receptor cysteine-rich domain / SRCR domain / SRCR domain profile. / SRCR-like domain / SRCR-like domain superfamily / Scavenger receptor Cys-rich / Low-density lipoprotein (LDL) receptor class A, conserved site / LDL-receptor class A (LDLRA) domain signature. / LDL-receptor class A (LDLRA) domain profile. / Low-density lipoprotein receptor domain class A ...Scavenger receptor cysteine-rich domain / SRCR domain / SRCR domain profile. / SRCR-like domain / SRCR-like domain superfamily / Scavenger receptor Cys-rich / Low-density lipoprotein (LDL) receptor class A, conserved site / LDL-receptor class A (LDLRA) domain signature. / LDL-receptor class A (LDLRA) domain profile. / Low-density lipoprotein receptor domain class A / Low-density lipoprotein (LDL) receptor class A repeat / LDL receptor-like superfamily / Serine proteases, trypsin family, histidine active site / Serine proteases, trypsin family, serine active site / Peptidase S1A, chymotrypsin family / Serine proteases, trypsin family, histidine active site. / Serine proteases, trypsin domain profile. / Serine proteases, trypsin family, serine active site. / Trypsin-like serine protease / Serine proteases, trypsin domain / Trypsin / Peptidase S1, PA clan, chymotrypsin-like fold / Peptidase S1, PA clan
Similarity search - Domain/homology
4-carbamimidamidobenzoic acid / Transmembrane protease serine 2
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.39 Å
AuthorsWang, H. / Duan, Y. / Liu, X. / Sun, L. / Yang, H.
Funding support China, 1items
OrganizationGrant numberCountry
National Natural Science Foundation of China (NSFC)92169109 China
CitationJournal: To Be Published
Title: Crystal structure of TMPRSS2 in complex with Camostat
Authors: Wang, H. / Duan, Y. / Liu, X. / Sun, L. / Yang, H.
History
DepositionJun 4, 2022Deposition site: PDBJ / Processing site: PDBJ
Revision 1.0Dec 6, 2023Provider: repository / Type: Initial release

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: Transmembrane protease serine 2 catalytic chain
C: Transmembrane protease serine 2 catalytic chain
B: Transmembrane protease serine 2 catalytic chain
D: Transmembrane protease serine 2 catalytic chain
hetero molecules


Theoretical massNumber of molelcules
Total (without water)88,79611
Polymers87,8234
Non-polymers9737
Water2,774154
1
A: Transmembrane protease serine 2 catalytic chain
C: Transmembrane protease serine 2 catalytic chain
hetero molecules


Theoretical massNumber of molelcules
Total (without water)44,3525
Polymers43,9112
Non-polymers4403
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area2700 Å2
ΔGint-9 kcal/mol
Surface area16410 Å2
MethodPISA
2
B: Transmembrane protease serine 2 catalytic chain
D: Transmembrane protease serine 2 catalytic chain
hetero molecules


Theoretical massNumber of molelcules
Total (without water)44,4446
Polymers43,9112
Non-polymers5334
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area2700 Å2
ΔGint-7 kcal/mol
Surface area15880 Å2
MethodPISA
Unit cell
Length a, b, c (Å)49.157, 93.537, 92.350
Angle α, β, γ (deg.)90.00, 100.08, 90.00
Int Tables number4
Space group name H-MP1211

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Components

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Transmembrane protease serine 2 catalytic ... , 2 types, 4 molecules ABCD

#1: Protein Transmembrane protease serine 2 catalytic chain


Mass: 16054.661 Da / Num. of mol.: 2 / Mutation: Residues 250-255 SSRQSR were replaced with DDDDK.
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: TMPRSS2, PRSS10 / Production host: Spodoptera frugiperda (fall armyworm) / References: UniProt: O15393
#2: Protein Transmembrane protease serine 2 catalytic chain


Mass: 27856.742 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: TMPRSS2, PRSS10 / Production host: Spodoptera frugiperda (fall armyworm) / References: UniProt: O15393

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Sugars , 1 types, 2 molecules

#3: Sugar ChemComp-NAG / 2-acetamido-2-deoxy-beta-D-glucopyranose / N-acetyl-beta-D-glucosamine / 2-acetamido-2-deoxy-beta-D-glucose / 2-acetamido-2-deoxy-D-glucose / 2-acetamido-2-deoxy-glucose / N-ACETYL-D-GLUCOSAMINE / N-Acetylglucosamine


Type: D-saccharide, beta linking / Mass: 221.208 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C8H15NO6
IdentifierTypeProgram
DGlcpNAcbCONDENSED IUPAC CARBOHYDRATE SYMBOLGMML 1.0
N-acetyl-b-D-glucopyranosamineCOMMON NAMEGMML 1.0
b-D-GlcpNAcIUPAC CARBOHYDRATE SYMBOLPDB-CARE 1.0
GlcNAcSNFG CARBOHYDRATE SYMBOLGMML 1.0

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Non-polymers , 4 types, 159 molecules

#4: Chemical ChemComp-CA / CALCIUM ION


Mass: 40.078 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Formula: Ca
#5: Chemical ChemComp-GBS / 4-carbamimidamidobenzoic acid / Nafamostat, bound form / Nafamostat


Mass: 179.176 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C8H9N3O2 / Feature type: SUBJECT OF INVESTIGATION
Comment: anticancer, anticoagulant, antivirus, protease inhibitor*YM
#6: Chemical ChemComp-GOL / GLYCEROL / GLYCERIN / PROPANE-1,2,3-TRIOL / Glycerol


Mass: 92.094 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C3H8O3
#7: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 154 / Source method: isolated from a natural source / Formula: H2O

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Details

Has ligand of interestY
Sequence detailsChains A and C, as well as B and D, were manipulated as one single peptide, but auto-cleaved at ...Chains A and C, as well as B and D, were manipulated as one single peptide, but auto-cleaved at residue 256 during zymogen activation.

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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: 2.36 Å3/Da / Density % sol: 47.9 % / Description: Plate
Crystal growTemperature: 293 K / Method: vapor diffusion, hanging drop
Details: 0.1M acetic acid/sodium acetate, pH 5.0, 16% w/v PEG 8000

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: SSRF / Beamline: BL02U1 / Wavelength: 0.979183 Å
DetectorType: DECTRIS EIGER2 S 9M / Detector: PIXEL / Date: Jan 10, 2022
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.979183 Å / Relative weight: 1
ReflectionResolution: 2.39→45.46 Å / Num. obs: 32630 / % possible obs: 99.5 % / Redundancy: 4.02 % / CC1/2: 0.996 / Rmerge(I) obs: 0.103 / Rrim(I) all: 0.119 / Net I/σ(I): 10.17
Reflection shell
Resolution (Å)Rmerge(I) obsNum. unique obsCC1/2Rrim(I) allDiffraction-ID
2.39-2.530.73552200.8060.8431
2.53-2.710.49649430.9010.5721
2.71-2.920.33546170.9370.3881
2.92-3.20.19842420.9750.2281
3.2-3.580.11438270.9910.131
3.58-4.130.07134030.9950.0821
4.13-5.060.05128830.9970.0591
5.06-7.140.05322460.9960.0611
7.14-45.460.03912490.9970.0451

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Processing

Software
NameVersionClassification
PHENIX1.20.1_4487refinement
XDS2020-12-02data scaling
PDB_EXTRACT3.27data extraction
XDS2020-12-02data reduction
PHENIX1.18.2_3874phasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: Model predicted by Alphafold

Resolution: 2.39→45.46 Å / SU ML: 0.33 / Cross valid method: THROUGHOUT / σ(F): 1.35 / Phase error: 26.72 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2394 1998 6.13 %
Rwork0.1951 --
obs0.1979 32610 99.5 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.1 Å / Solvent model: FLAT BULK SOLVENT MODEL
Refinement stepCycle: LAST / Resolution: 2.39→45.46 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms5576 0 60 155 5791
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0025789
X-RAY DIFFRACTIONf_angle_d0.5277892
X-RAY DIFFRACTIONf_dihedral_angle_d6.734802
X-RAY DIFFRACTIONf_chiral_restr0.046853
X-RAY DIFFRACTIONf_plane_restr0.0041017
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2.39-2.450.37131420.31232175X-RAY DIFFRACTION99
2.45-2.510.31841400.27722148X-RAY DIFFRACTION99
2.51-2.590.33741450.25592197X-RAY DIFFRACTION99
2.59-2.670.32791390.24832131X-RAY DIFFRACTION99
2.67-2.770.26551430.23082210X-RAY DIFFRACTION100
2.77-2.880.2771420.22542176X-RAY DIFFRACTION100
2.88-3.010.28081430.22872184X-RAY DIFFRACTION100
3.01-3.170.26641410.21092166X-RAY DIFFRACTION100
3.17-3.370.26091440.19112194X-RAY DIFFRACTION100
3.37-3.630.23971420.18682197X-RAY DIFFRACTION100
3.63-3.990.21121430.17672180X-RAY DIFFRACTION100
3.99-4.570.20321450.15622216X-RAY DIFFRACTION100
4.57-5.750.19111430.17042199X-RAY DIFFRACTION100
5.75-45.460.20581460.17942239X-RAY DIFFRACTION99

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