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- PDB-5wv8: Crystal structure of a mutant insect group III chitinase (CAD1-E2... -

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Basic information

Entry
Database: PDB / ID: 5wv8
TitleCrystal structure of a mutant insect group III chitinase (CAD1-E217L) from Ostrinia furnacalis
ComponentsChitinase
KeywordsHYDROLASE / Ostrinia furnacalis / chitinase / three-dimensional structure / chitin metabolism
Function / homology
Function and homology information


endochitinase activity / chitinase / chitin catabolic process / chitin binding / carbohydrate metabolic process / extracellular region
Similarity search - Function
Chitin-binding domain type 2 / Chitin binding domain / Chitin binding Peritrophin-A domain / Chitin-binding type-2 domain profile. / Chitin binding domain superfamily / Glycosyl hydrolases family 18 (GH18) active site / Glycosyl hydrolases family 18 (GH18) active site signature. / : / Chitinase insertion domain superfamily / Chitinase II ...Chitin-binding domain type 2 / Chitin binding domain / Chitin binding Peritrophin-A domain / Chitin-binding type-2 domain profile. / Chitin binding domain superfamily / Glycosyl hydrolases family 18 (GH18) active site / Glycosyl hydrolases family 18 (GH18) active site signature. / : / Chitinase insertion domain superfamily / Chitinase II / Glyco_18 / Glycosyl hydrolases family 18 / Glycosyl hydrolases family 18 (GH18) domain profile. / Glycoside hydrolase family 18, catalytic domain / Glycoside hydrolase superfamily
Similarity search - Domain/homology
Biological speciesOstrinia furnacalis (Asian corn borer)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.042 Å
AuthorsLiu, T. / Zhou, Y. / Yang, Q.
Funding support China, 4items
OrganizationGrant numberCountry
National Natural Science Foundation of China31425021 China
Ministry of Education of the People's Republic of ChinaLJQ2014006 China
National Natural Science Foundation of China61202252 China
Dalian University of TechnologyDUT16QY48 China
CitationJournal: Acta Crystallogr D Struct Biol / Year: 2018
Title: The deduced role of a chitinase containing two nonsynergistic catalytic domains
Authors: Liu, T. / Zhu, W. / Wang, J. / Zhou, Y. / Duan, Y. / Qu, M. / Yang, Q.
History
DepositionDec 22, 2016Deposition site: PDBJ / Processing site: PDBJ
Revision 1.0Dec 27, 2017Provider: repository / Type: Initial release
Revision 1.1Jan 16, 2019Group: Data collection / Database references / Category: citation / citation_author
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
Revision 1.2Nov 22, 2023Group: Data collection / Database references / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession
Revision 1.3Nov 6, 2024Group: Structure summary / Category: pdbx_entry_details / pdbx_modification_feature

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: Chitinase


Theoretical massNumber of molelcules
Total (without water)54,0261
Polymers54,0261
Non-polymers00
Water6,467359
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area0 Å2
ΔGint0 kcal/mol
Surface area16030 Å2
Unit cell
Length a, b, c (Å)72.100, 72.100, 192.997
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number92
Space group name H-MP41212

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Components

#1: Protein Chitinase


Mass: 54026.371 Da / Num. of mol.: 1 / Fragment: UNP residues 1-482 / Mutation: E217L
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Ostrinia furnacalis (Asian corn borer) / Production host: Komagataella pastoris CBS 7435 (fungus) / References: UniProt: U5LUV7, chitinase
#2: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 359 / 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: 2.32 Å3/Da / Density % sol: 47.01 %
Crystal growTemperature: 277 K / Method: vapor diffusion, hanging drop / pH: 6.6
Details: 200mM ammonium sulfate, 100mM Bis-Tris pH 6.6, 21% PEG 3350

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: SSRF / Beamline: BL17U / Wavelength: 1 Å
DetectorType: ADSC QUANTUM 315r / Detector: CCD / Date: Oct 16, 2014
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 2.03→50 Å / Num. obs: 35271 / % possible obs: 94.4 % / Redundancy: 14.1 % / Rsym value: 0.0765 / Net I/σ(I): 10.6
Reflection shellResolution: 2.03→2.07 Å / Redundancy: 12.7 % / Rsym value: 0.371 / % possible all: 85

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Processing

Software
NameVersionClassification
PHENIX1.9_1692refinement
HKL-2000data reduction
HKL-2000data scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 5wup

5wup


Resolution: 2.042→40.099 Å / SU ML: 0.17 / Cross valid method: FREE R-VALUE / σ(F): 1.34 / Phase error: 17.91
RfactorNum. reflection% reflection
Rfree0.19 2000 6.03 %
Rwork0.1645 --
obs0.1661 33179 99.76 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å
Refinement stepCycle: LAST / Resolution: 2.042→40.099 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms3115 0 0 359 3474
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0073210
X-RAY DIFFRACTIONf_angle_d0.9874340
X-RAY DIFFRACTIONf_dihedral_angle_d13.5371181
X-RAY DIFFRACTIONf_chiral_restr0.048441
X-RAY DIFFRACTIONf_plane_restr0.004557
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2.0424-2.09340.21061360.1872111X-RAY DIFFRACTION97
2.0934-2.150.19211400.18032191X-RAY DIFFRACTION100
2.15-2.21330.22711410.17272191X-RAY DIFFRACTION100
2.2133-2.28470.22561390.1662184X-RAY DIFFRACTION100
2.2847-2.36640.16541410.17672189X-RAY DIFFRACTION100
2.3664-2.46110.22951410.17292204X-RAY DIFFRACTION100
2.4611-2.57310.20211420.17482220X-RAY DIFFRACTION100
2.5731-2.70870.24191420.18272196X-RAY DIFFRACTION100
2.7087-2.87840.23071410.18312219X-RAY DIFFRACTION100
2.8784-3.10060.20441440.17552227X-RAY DIFFRACTION100
3.1006-3.41240.20531440.16922250X-RAY DIFFRACTION100
3.4124-3.90590.16181440.14452251X-RAY DIFFRACTION100
3.9059-4.91950.12931490.13142309X-RAY DIFFRACTION100
4.9195-40.10660.1971560.17262437X-RAY DIFFRACTION99

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