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- PDB-7jqv: Crystal structure of the R64F mutant of Bauhinia Bauhinioides Kal... -

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Basic information

Entry
Database: PDB / ID: 7jqv
TitleCrystal structure of the R64F mutant of Bauhinia Bauhinioides Kallikrein Inhibitor complexed with Human Kallikrein 4
Components
  • Kallikrein 4 (Prostase, enamel matrix, prostate), isoform CRA_a
  • Kunitz-type inihibitor
KeywordsHYDROLASE/INHIBITOR / Human Kallikrein 4 / Bauhinia Bauhiniordes Kallikrein Inhibitor / STRUCTURAL PROTEIN / HYDROLASE-INHIBITOR complex
Function / homology
Function and homology information


biomineral tissue development / amelogenesis / endopeptidase inhibitor activity / extracellular matrix disassembly / protein catabolic process / serine-type endopeptidase activity / proteolysis / extracellular region / metal ion binding
Similarity search - Function
Proteinase inhibitor I3, Kunitz legume / Trypsin and protease inhibitor / Soybean trypsin inhibitor (Kunitz) family of protease inhibitors / Kunitz inhibitor STI-like superfamily / 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. ...Proteinase inhibitor I3, Kunitz legume / Trypsin and protease inhibitor / Soybean trypsin inhibitor (Kunitz) family of protease inhibitors / Kunitz inhibitor STI-like superfamily / 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
Kallikrein-4 / Kunitz-type inihibitor
Similarity search - Component
Biological speciesHomo sapiens (human)
Bauhinia bauhinioides (plant)
MethodX-RAY DIFFRACTION / SYNCHROTRON / FOURIER SYNTHESIS / Resolution: 2.1 Å
AuthorsLi, M. / Wlodawer, A. / Gustchina, A.
CitationJournal: Acta Crystallogr D Struct Biol / Year: 2021
Title: Structural studies of complexes of kallikrein 4 with wild-type and mutated forms of the Kunitz-type inhibitor BbKI.
Authors: Li, M. / Srp, J. / Mares, M. / Wlodawer, A. / Gustchina, A.
History
DepositionAug 11, 2020Deposition site: RCSB / Processing site: RCSB
Revision 1.0Jul 21, 2021Provider: repository / Type: Initial release
Revision 1.1Aug 11, 2021Group: Database references / Category: citation / citation_author / database_2
Item: _citation.journal_abbrev / _citation.journal_id_CSD ..._citation.journal_abbrev / _citation.journal_id_CSD / _citation.journal_id_ISSN / _citation.journal_volume / _citation.page_first / _citation.page_last / _citation.pdbx_database_id_DOI / _citation.pdbx_database_id_PubMed / _citation.title / _citation.year / _citation_author.identifier_ORCID / _citation_author.name / _database_2.pdbx_DOI / _database_2.pdbx_database_accession
Revision 1.2Nov 20, 2024Group: Data collection / Structure summary
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / pdbx_entry_details / pdbx_modification_feature
Item: _pdbx_entry_details.has_protein_modification

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
E: Kallikrein 4 (Prostase, enamel matrix, prostate), isoform CRA_a
I: Kunitz-type inihibitor
hetero molecules


Theoretical massNumber of molelcules
Total (without water)43,3717
Polymers42,0572
Non-polymers1,3145
Water9,188510
1


  • Idetical with deposited unit
  • defined by author&software
  • Evidence: gel filtration
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area2560 Å2
ΔGint-34 kcal/mol
Surface area17160 Å2
MethodPISA
Unit cell
Length a, b, c (Å)103.790, 103.790, 86.005
Angle α, β, γ (deg.)90.000, 90.000, 120.000
Int Tables number152
Space group name H-MP3121
Components on special symmetry positions
IDModelComponents
11E-452-

HOH

21E-492-

HOH

31I-1065-

HOH

41I-1090-

HOH

51I-1103-

HOH

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Components

#1: Protein Kallikrein 4 (Prostase, enamel matrix, prostate), isoform CRA_a / Kallikrein B1 / Kallikrein-4


Mass: 23926.010 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: KLK4, KLNB1, hCG_1641510 / Production host: Escherichia coli (E. coli) / References: UniProt: A0A0C4DFQ5
#2: Protein Kunitz-type inihibitor


Mass: 18130.498 Da / Num. of mol.: 1 / Mutation: R64F
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Bauhinia bauhinioides (plant) / Production host: Escherichia coli (E. coli) / References: UniProt: Q6VEQ7
#3: Chemical ChemComp-2PE / NONAETHYLENE GLYCOL


Mass: 414.488 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: C18H38O10 / Comment: precipitant*YM
#4: Chemical ChemComp-CL / CHLORIDE ION


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


Mass: 18.015 Da / Num. of mol.: 510 / Source method: isolated from a natural source / Formula: H2O
Has ligand of interestN
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: 3.18 Å3/Da / Density % sol: 61.32 %
Crystal growTemperature: 293 K / Method: vapor diffusion, hanging drop / Details: 2.0M Ammonium Sulfate, 2% PEG400, 10mM CdCl2

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 22-ID / Wavelength: 1 Å
DetectorType: DECTRIS EIGER X 16M / Detector: PIXEL / Date: Dec 19, 2019
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 2.1→89.88 Å / Num. obs: 31637 / % possible obs: 100 % / Redundancy: 22.5 % / Rsym value: 0.119 / Net I/σ(I): 11.1
Reflection shellResolution: 2.1→2.16 Å / Num. unique obs: 2569 / Rsym value: 0.703

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Processing

Software
NameVersionClassification
REFMAC5.8.0258refinement
PDB_EXTRACT3.25data extraction
XDSdata reduction
Aimlessdata scaling
REFMACphasing
RefinementMethod to determine structure: FOURIER SYNTHESIS / Resolution: 2.1→30 Å / Cor.coef. Fo:Fc: 0.974 / Cor.coef. Fo:Fc free: 0.956 / SU B: 4.018 / SU ML: 0.106 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.143 / ESU R Free: 0.142 / Stereochemistry target values: MAXIMUM LIKELIHOOD
Details: HYDROGENS HAVE BEEN USED IF PRESENT IN THE INPUT U VALUES : REFINED INDIVIDUALLY
RfactorNum. reflection% reflectionSelection details
Rfree0.197 944 3 %RANDOM
Rwork0.1451 ---
obs0.1467 30650 99.94 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: BABINET MODEL WITH MASK
Displacement parametersBiso max: 189.09 Å2 / Biso mean: 46.793 Å2 / Biso min: 15.6 Å2
Baniso -1Baniso -2Baniso -3
1--0.55 Å2-0.27 Å2-0 Å2
2---0.55 Å20 Å2
3---1.78 Å2
Refinement stepCycle: final / Resolution: 2.1→30 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms2951 0 35 510 3496
Biso mean--80.42 61.77 -
Num. residues----389
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0160.0123109
X-RAY DIFFRACTIONr_angle_refined_deg2.2581.6264226
X-RAY DIFFRACTIONr_dihedral_angle_1_deg7.4895396
X-RAY DIFFRACTIONr_dihedral_angle_2_deg38.49224.296142
X-RAY DIFFRACTIONr_dihedral_angle_3_deg15.96615504
X-RAY DIFFRACTIONr_dihedral_angle_4_deg24.1161510
X-RAY DIFFRACTIONr_chiral_restr0.1550.2395
X-RAY DIFFRACTIONr_gen_planes_refined0.0150.022369
LS refinement shellResolution: 2.1→2.154 Å / Rfactor Rfree error: 0 / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.268 60 -
Rwork0.209 2219 -
all-2279 -
obs--100 %

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