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- PDB-4x1q: The crystal structure of mupain-1 in complex with murinised human... -

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Basic information

Entry
Database: PDB / ID: 4x1q
TitleThe crystal structure of mupain-1 in complex with murinised human uPA at pH7.4
Components
  • Urokinase-type plasminogen activator
  • mupain-1
KeywordsHYDROLASE INHIBITOR/HYDROLASE / Serine protease / peptidic inhibitor / uPA / HYDROLASE INHIBITOR-HYDROLASE complex
Function / homology
Function and homology information


u-plasminogen activator / regulation of smooth muscle cell-matrix adhesion / urokinase plasminogen activator signaling pathway / regulation of plasminogen activation / regulation of fibrinolysis / regulation of wound healing / protein complex involved in cell-matrix adhesion / negative regulation of plasminogen activation / regulation of smooth muscle cell migration / regulation of signaling receptor activity ...u-plasminogen activator / regulation of smooth muscle cell-matrix adhesion / urokinase plasminogen activator signaling pathway / regulation of plasminogen activation / regulation of fibrinolysis / regulation of wound healing / protein complex involved in cell-matrix adhesion / negative regulation of plasminogen activation / regulation of smooth muscle cell migration / regulation of signaling receptor activity / serine-type endopeptidase complex / Dissolution of Fibrin Clot / smooth muscle cell migration / plasminogen activation / regulation of cell adhesion mediated by integrin / tertiary granule membrane / negative regulation of fibrinolysis / regulation of cell adhesion / specific granule membrane / serine protease inhibitor complex / fibrinolysis / chemotaxis / blood coagulation / regulation of cell population proliferation / response to hypoxia / positive regulation of cell migration / external side of plasma membrane / serine-type endopeptidase activity / focal adhesion / Neutrophil degranulation / cell surface / signal transduction / proteolysis / extracellular space / extracellular exosome / extracellular region / plasma membrane
Similarity search - Function
Kringle domain / Kringle / Kringle, conserved site / Kringle superfamily / Kringle domain signature. / Kringle domain profile. / Kringle domain / : / Kringle-like fold / EGF-like domain profile. ...Kringle domain / Kringle / Kringle, conserved site / Kringle superfamily / Kringle domain signature. / Kringle domain profile. / Kringle domain / : / Kringle-like fold / EGF-like domain profile. / EGF-like domain signature 1. / EGF-like domain / 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 / Trypsin-like serine proteases / Thrombin, subunit H / Peptidase S1, PA clan, chymotrypsin-like fold / Peptidase S1, PA clan / Beta Barrel / Mainly Beta
Similarity search - Domain/homology
Urokinase-type plasminogen activator
Similarity search - Component
Biological speciesHomo sapiens (human)
synthetic construct (others)
MethodX-RAY DIFFRACTION / SYNCHROTRON / Resolution: 2.28 Å
AuthorsJiang, L. / Zhao, B. / Xu, P. / Andreasen, P. / Huang, M.
Funding support China, Denmark, 4items
OrganizationGrant numberCountry
the National Natural Science Foundation of China31161130356 China
the National Natural Science Foundation of China30770429 China
the Natural Science Foundation of Fujian Province2012J05071 China
the Danish National Research Foundation26-331-6 Denmark
CitationJournal: Plos One / Year: 2014
Title: A cyclic peptidic serine protease inhibitor: increasing affinity by increasing peptide flexibility.
Authors: Zhao, B. / Xu, P. / Jiang, L. / Paaske, B. / Kromann-Hansen, T. / Jensen, J.K. / Srensen, H.P. / Liu, Z. / Nielsen, J.T. / Christensen, A. / Hosseini, M. / Srensen, K.K. / Nielsen, N.C. / ...Authors: Zhao, B. / Xu, P. / Jiang, L. / Paaske, B. / Kromann-Hansen, T. / Jensen, J.K. / Srensen, H.P. / Liu, Z. / Nielsen, J.T. / Christensen, A. / Hosseini, M. / Srensen, K.K. / Nielsen, N.C. / Jensen, K.J. / Huang, M. / Andreasen, P.A.
History
DepositionNov 25, 2014Deposition site: RCSB / Processing site: PDBJ
Revision 1.0Mar 25, 2015Provider: repository / Type: Initial release
Revision 1.1Nov 4, 2015Group: Experimental preparation

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
P: mupain-1
U: Urokinase-type plasminogen activator


Theoretical massNumber of molelcules
Total (without water)29,0612
Polymers29,0612
Non-polymers00
Water36020
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area1470 Å2
ΔGint-5 kcal/mol
Surface area11140 Å2
MethodPISA
Unit cell
Length a, b, c (Å)122.105, 122.105, 42.546
Angle α, β, γ (deg.)90.00, 90.00, 120.00
Int Tables number146
Space group name H-MH3

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Components

#1: Protein/peptide mupain-1


Mass: 1191.358 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) synthetic construct (others)
#2: Protein Urokinase-type plasminogen activator / uPA


Mass: 27869.742 Da / Num. of mol.: 1 / Fragment: catalytic domain (UNP RESIDUES 179-425) / Mutation: H99Y, C122A, N145Q
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: PLAU / Production host: Komagataella pastoris (fungus) / References: UniProt: P00749, u-plasminogen activator
#3: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 20 / Source method: isolated from a natural source / Formula: H2O

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION

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Sample preparation

CrystalDensity Matthews: 2.1 Å3/Da / Density % sol: 41.44 %
Crystal growTemperature: 298 K / Method: vapor diffusion, sitting drop / pH: 4.6
Details: 2.0M ammonium sulfate, 50mM sodium citrate pH 4.6, 5% PEG 400

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: SSRF / Beamline: BL17U / Wavelength: 0.979 Å
DetectorType: ADSC QUANTUM 315 / Detector: CCD / Date: Jan 25, 2013
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.979 Å / Relative weight: 1
ReflectionResolution: 2.28→60 Å / Num. obs: 10700 / % possible obs: 99.6 % / Redundancy: 3.6 % / Net I/σ(I): 34.1

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Processing

Software
NameVersionClassification
REFMAC5.5.0110refinement
Cootdata reduction
RefinementResolution: 2.28→60 Å / Cor.coef. Fo:Fc: 0.949 / Cor.coef. Fo:Fc free: 0.893 / SU B: 9.091 / SU ML: 0.225 / Cross valid method: THROUGHOUT / ESU R: 0.491 / ESU R Free: 0.3 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
RfactorNum. reflection% reflectionSelection details
Rfree0.2868 510 4.8 %RANDOM
Rwork0.20521 ---
obs0.20886 10186 99.42 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: MASK
Displacement parametersBiso mean: 44.22 Å2
Baniso -1Baniso -2Baniso -3
1--0.82 Å2-0.41 Å20 Å2
2---0.82 Å20 Å2
3---1.23 Å2
Refinement stepCycle: LAST / Resolution: 2.28→60 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms2034 0 0 20 2054
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0170.0222098
X-RAY DIFFRACTIONr_bond_other_d
X-RAY DIFFRACTIONr_angle_refined_deg1.7491.9492846
X-RAY DIFFRACTIONr_angle_other_deg
X-RAY DIFFRACTIONr_dihedral_angle_1_deg7.3365256
X-RAY DIFFRACTIONr_dihedral_angle_2_deg35.96423.15292
X-RAY DIFFRACTIONr_dihedral_angle_3_deg19.80515353
X-RAY DIFFRACTIONr_dihedral_angle_4_deg21.4341514
X-RAY DIFFRACTIONr_chiral_restr0.1240.2304
X-RAY DIFFRACTIONr_gen_planes_refined0.0080.0211585
X-RAY DIFFRACTIONr_gen_planes_other
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_it1.1691.51280
X-RAY DIFFRACTIONr_mcbond_other
X-RAY DIFFRACTIONr_mcangle_it2.20222070
X-RAY DIFFRACTIONr_mcangle_other
X-RAY DIFFRACTIONr_scbond_it2.9113818
X-RAY DIFFRACTIONr_scbond_other
X-RAY DIFFRACTIONr_scangle_it4.7534.5776
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: 2.284→2.343 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.378 34 -
Rwork0.231 753 -
obs--97.16 %

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