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- PDB-5wvf: Crystal structure of a mutant insect group III chitinase (CAD2-E6... -

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Basic information

Entry
Database: PDB / ID: 5wvf
TitleCrystal structure of a mutant insect group III chitinase (CAD2-E647L) from Ostrinia furnacalis
ComponentsChitinase
KeywordsHYDROLASE / Ostrinia furnacalis / chitinase / three-dimensional structure / chitin metabolism
Function / homology
Function and homology information


chitinase / chitinase activity / 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 / Glyco_18 ...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 (GH18) domain profile. / Glycoside hydrolase family 18, catalytic domain / Glycosyl hydrolases family 18 / Glycoside hydrolase superfamily
Similarity search - Domain/homology
Biological speciesOstrinia furnacalis (Asian corn borer)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.399 Å
AuthorsLiu, T. / Zhou, Y. / Yang, Q.
Funding support China, 4items
OrganizationGrant numberCountry
National Natural Science Foundation of China31425021 China
National Natural Science Foundation of China61202252 China
Ministry of Education of the People's Republic of ChinaLJQ2014006 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 24, 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 1.2Jul 29, 2020Group: Data collection / Derived calculations / Structure summary
Category: chem_comp / entity ...chem_comp / entity / pdbx_chem_comp_identifier / pdbx_entity_nonpoly / struct_conn / struct_site / struct_site_gen
Item: _chem_comp.name / _chem_comp.type ..._chem_comp.name / _chem_comp.type / _entity.pdbx_description / _pdbx_entity_nonpoly.name / _struct_conn.pdbx_role
Description: Carbohydrate remediation / Provider: repository / Type: Remediation
Revision 1.3Nov 22, 2023Group: Data collection / Database references ...Data collection / Database references / Refinement description / Structure summary
Category: chem_comp / chem_comp_atom ...chem_comp / chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model
Item: _chem_comp.pdbx_synonyms / _database_2.pdbx_DOI / _database_2.pdbx_database_accession

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Chitinase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)52,6312
Polymers52,4101
Non-polymers2211
Water1,820101
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area160 Å2
ΔGint2 kcal/mol
Surface area15990 Å2
Unit cell
Length a, b, c (Å)71.475, 71.475, 175.985
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number92
Space group name H-MP41212
Components on special symmetry positions
IDModelComponents
11A-1174-

HOH

21A-1196-

HOH

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Components

#1: Protein Chitinase /


Mass: 52409.617 Da / Num. of mol.: 1 / Fragment: UNP residues 528-987 / Mutation: E647L
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: 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.: 1
Source method: isolated from a genetically manipulated source
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
#3: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 101 / Source method: isolated from a natural source / Formula: H2O

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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: 2.14 Å3/Da / Density % sol: 42.64 %
Crystal growTemperature: 277 K / Method: vapor diffusion, hanging drop / pH: 8.1 / Details: 200mM tri-sodium citrate dihydrate, 20% PEG3350

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: SSRF / Beamline: BL17U / Wavelength: 0.97915 Å
DetectorType: ADSC QUANTUM 315r / Detector: CCD / Date: Jun 15, 2015
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.97915 Å / Relative weight: 1
ReflectionResolution: 2.399→30 Å / Num. obs: 18731 / % possible obs: 99.6 % / Redundancy: 13.5 % / Rsym value: 0.067 / Net I/σ(I): 11.1
Reflection shellResolution: 2.399→2.44 Å / Redundancy: 13.9 % / Rsym value: 0.381 / % possible all: 100

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Processing

Software
NameVersionClassification
PHENIX(1.11_2567: ???)refinement
HKL-3000data reduction
HKL-3000data scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 5wus

5wus


Resolution: 2.399→28.883 Å / SU ML: 0.24 / Cross valid method: FREE R-VALUE / σ(F): 1.34 / Phase error: 22.77 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2328 1854 10 %
Rwork0.2068 --
obs0.2095 18540 99.43 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Refinement stepCycle: LAST / Resolution: 2.399→28.883 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms3004 0 14 101 3119
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0083101
X-RAY DIFFRACTIONf_angle_d1.1354203
X-RAY DIFFRACTIONf_dihedral_angle_d17.0931138
X-RAY DIFFRACTIONf_chiral_restr0.054439
X-RAY DIFFRACTIONf_plane_restr0.006545
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2.3985-2.46330.33641400.26311261X-RAY DIFFRACTION100
2.4633-2.53580.28091390.25091251X-RAY DIFFRACTION100
2.5358-2.61760.25911380.25171244X-RAY DIFFRACTION100
2.6176-2.7110.31281420.23631270X-RAY DIFFRACTION100
2.711-2.81950.24881390.231258X-RAY DIFFRACTION100
2.8195-2.94770.271420.24591276X-RAY DIFFRACTION100
2.9477-3.10290.30611400.24671268X-RAY DIFFRACTION100
3.1029-3.29710.26221420.22551269X-RAY DIFFRACTION100
3.2971-3.55130.27331430.20371287X-RAY DIFFRACTION100
3.5513-3.90790.21381450.18571302X-RAY DIFFRACTION100
3.9079-4.47150.18071430.16221293X-RAY DIFFRACTION99
4.4715-5.62680.15241460.17121315X-RAY DIFFRACTION99
5.6268-28.88520.22711550.20931392X-RAY DIFFRACTION98
Refinement TLS params.Method: refined / Origin x: -9.2492 Å / Origin y: 17.2832 Å / Origin z: 18.2217 Å
111213212223313233
T0.2686 Å20.0173 Å20.0009 Å2-0.1918 Å20.0842 Å2--0.2417 Å2
L2.0499 °21.1461 °20.7385 °2-3.7561 °20.8176 °2--2.3489 °2
S0.0453 Å °0.0769 Å °-0.1257 Å °-0.153 Å °-0.0878 Å °-0.3873 Å °-0.0547 Å °0.2089 Å °0.0374 Å °
Refinement TLS groupSelection details: all

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