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- PDB-5x1k: Vanillate/3-O-methylgallate O-demethylase, LigM, 3-O-methylgallat... -

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Basic information

Entry
Database: PDB / ID: 5x1k
TitleVanillate/3-O-methylgallate O-demethylase, LigM, 3-O-methylgallate complex form
ComponentsVanillate/3-O-methylgallate O-demethylase
KeywordsOXIDOREDUCTASE / Lignin / Sphingobium sp.SYK-6
Function / homology
Function and homology information


vanillate/3-O-methylgallate O-demethylase / lignin catabolic process / methyltransferase activity / methylation
Similarity search - Function
Aminomethyltransferase-like / Aminomethyltransferase, folate-binding domain / Aminomethyltransferase folate-binding domain / GTP-binding protein TrmE/Aminomethyltransferase GcvT, domain 1
Similarity search - Domain/homology
3-methoxy-4,5-bis(oxidanyl)benzoic acid / DI(HYDROXYETHYL)ETHER / Vanillate/3-O-methylgallate O-demethylase
Similarity search - Component
Biological speciesSphingobium sp. SYK-6 (bacteria)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.15 Å
AuthorsHarada, A. / Senda, T.
Funding support Japan, 3items
OrganizationGrant numberCountry
Japan Society for the Promotion of Science14J04356 Japan
the Ministry of Education, Culture, Sports, Science and TechnologyPlatform for Drug Discovery, Informatics, and Structural Life Science Japan
Japan Agency for Medical Research and Development (AMED)Platform for Drug Discovery, Informatics, and Structural Life Science Japan
CitationJournal: FEBS J. / Year: 2017
Title: The crystal structure of a new O-demethylase from Sphingobium sp. strain SYK-6
Authors: Harada, A. / Kamimura, N. / Takeuchi, K. / Yu, H.Y. / Masai, E. / Senda, T.
History
DepositionJan 26, 2017Deposition site: PDBJ / Processing site: PDBJ
Revision 1.0May 17, 2017Provider: repository / Type: Initial release
Revision 1.1May 31, 2017Group: Database references
Revision 1.2Jun 28, 2017Group: Database references / Category: citation
Item: _citation.country / _citation.journal_volume ..._citation.country / _citation.journal_volume / _citation.page_first / _citation.page_last
Revision 1.3Nov 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

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Vanillate/3-O-methylgallate O-demethylase
B: Vanillate/3-O-methylgallate O-demethylase
C: Vanillate/3-O-methylgallate O-demethylase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)158,98813
Polymers157,8363
Non-polymers1,15110
Water4,486249
1
A: Vanillate/3-O-methylgallate O-demethylase
hetero molecules

A: Vanillate/3-O-methylgallate O-demethylase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)106,42214
Polymers105,2242
Non-polymers1,19712
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation2_555-x,-y,z1
Buried area5600 Å2
ΔGint6 kcal/mol
Surface area33000 Å2
MethodPISA
2
B: Vanillate/3-O-methylgallate O-demethylase
C: Vanillate/3-O-methylgallate O-demethylase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)105,7776
Polymers105,2242
Non-polymers5534
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area4160 Å2
ΔGint-15 kcal/mol
Surface area32880 Å2
MethodPISA
Unit cell
Length a, b, c (Å)104.055, 118.066, 132.823
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number18
Space group name H-MP21212
Components on special symmetry positions
IDModelComponents
11A-704-

HOH

21A-742-

HOH

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Components

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Protein , 1 types, 3 molecules ABC

#1: Protein Vanillate/3-O-methylgallate O-demethylase


Mass: 52612.145 Da / Num. of mol.: 3
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Sphingobium sp. SYK-6 (bacteria) / Gene: ligM, SLG_12740 / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21(DE3) / References: UniProt: G2IQS7

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Non-polymers , 5 types, 259 molecules

#2: Chemical ChemComp-7WR / 3-methoxy-4,5-bis(oxidanyl)benzoic acid


Mass: 184.146 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: C8H8O5
#3: Chemical ChemComp-TRS / 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL / TRIS BUFFER


Mass: 122.143 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C4H12NO3 / Comment: pH buffer*YM
#4: Chemical ChemComp-PEG / DI(HYDROXYETHYL)ETHER


Mass: 106.120 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C4H10O3
#5: Chemical
ChemComp-EDO / 1,2-ETHANEDIOL / ETHYLENE GLYCOL


Mass: 62.068 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C2H6O2
#6: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 249 / 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: 2.6 Å3/Da / Density % sol: 52.62 %
Description: THE ENTRY CONTAINS FRIEDEL PAIRS IN F_PLUS/MINUS COLUMNS.
Crystal growTemperature: 293 K / Method: vapor diffusion, hanging drop / Details: 0.1M Tris pH 8.5, 0.1M LiCl, 30%(w/v) PEG8000

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Data collection

DiffractionMean temperature: 95 K
Diffraction sourceSource: SYNCHROTRON / Site: Photon Factory / Beamline: AR-NE3A / Wavelength: 1 Å
DetectorType: DECTRIS PILATUS 2M-F / Detector: PIXEL / Date: Dec 19, 2015
RadiationMonochromator: Si 111 / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 2.15→48.44 Å / Num. obs: 178538 / % possible obs: 99.7 % / Redundancy: 10.5 % / Net I/σ(I): 13.2
Reflection shellResolution: 2.15→2.19 Å / Mean I/σ(I) obs: 1.8 / % possible all: 97.3

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Processing

Software
NameVersionClassification
PHENIX(1.11.1_2575: ???)refinement
XDSdata reduction
Aimlessdata scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 5X1I

5x1i


Resolution: 2.15→44.818 Å / SU ML: 0.3 / Cross valid method: FREE R-VALUE / σ(F): 1.33 / Phase error: 29.01
Details: SF FILE CONTAINS FRIEDEL PAIRS UNDER I/F_MINUS AND I/F_PLUS COLUMNS.
RfactorNum. reflection% reflection
Rfree0.2744 8712 5.09 %
Rwork0.2325 --
obs0.2347 171292 99.61 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å
Refinement stepCycle: LAST / Resolution: 2.15→44.818 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms10083 0 78 249 10410
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00710452
X-RAY DIFFRACTIONf_angle_d0.90314261
X-RAY DIFFRACTIONf_dihedral_angle_d7.4677653
X-RAY DIFFRACTIONf_chiral_restr0.0551515
X-RAY DIFFRACTIONf_plane_restr0.0071869
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2.15-2.17440.36952680.32285268X-RAY DIFFRACTION96
2.1744-2.20.32563040.3015259X-RAY DIFFRACTION98
2.2-2.22690.32672940.30215356X-RAY DIFFRACTION98
2.2269-2.2550.33643090.29185311X-RAY DIFFRACTION98
2.255-2.28470.32482910.28865424X-RAY DIFFRACTION99
2.2847-2.3160.32513030.29125416X-RAY DIFFRACTION99
2.316-2.34910.35392690.28215422X-RAY DIFFRACTION100
2.3491-2.38420.32792970.28795409X-RAY DIFFRACTION100
2.3842-2.42140.32772820.26755540X-RAY DIFFRACTION100
2.4214-2.46110.30822820.26455414X-RAY DIFFRACTION100
2.4611-2.50350.34343280.26875364X-RAY DIFFRACTION100
2.5035-2.54910.27532890.26785466X-RAY DIFFRACTION100
2.5491-2.59810.30742790.26635443X-RAY DIFFRACTION100
2.5981-2.65110.313020.25465385X-RAY DIFFRACTION100
2.6511-2.70870.30072770.25215506X-RAY DIFFRACTION100
2.7087-2.77180.28352710.24385421X-RAY DIFFRACTION100
2.7718-2.84110.29732760.24775428X-RAY DIFFRACTION100
2.8411-2.91790.3132820.25235471X-RAY DIFFRACTION100
2.9179-3.00370.312740.25275454X-RAY DIFFRACTION100
3.0037-3.10060.28622910.24095419X-RAY DIFFRACTION100
3.1006-3.21140.26442570.23865497X-RAY DIFFRACTION100
3.2114-3.340.27212840.24115447X-RAY DIFFRACTION100
3.34-3.49190.29672660.23795496X-RAY DIFFRACTION100
3.4919-3.67590.28613250.22755411X-RAY DIFFRACTION100
3.6759-3.90610.25573000.215409X-RAY DIFFRACTION100
3.9061-4.20750.22992870.19065450X-RAY DIFFRACTION100
4.2075-4.63050.21642850.17655414X-RAY DIFFRACTION100
4.6305-5.29970.21593240.17395422X-RAY DIFFRACTION100
5.2997-6.67350.2363250.1975414X-RAY DIFFRACTION100
6.6735-44.82740.19762910.1785444X-RAY DIFFRACTION100

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