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- PDB-4pct: Crystal structure of a bacterial fucosidase with iminocyclitol (2... -

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Basic information

Entry
Database: PDB / ID: 4pct
TitleCrystal structure of a bacterial fucosidase with iminocyclitol (2S,3S,4R,5S)-3,4-dihydroxy-2-ethynyl-5-methylpyrrolidine
ComponentsAlpha-L-fucosidase
KeywordsHYDROLASE / enzyme inhibition
Function / homology
Function and homology information


alpha-L-fucosidase activity / fucose metabolic process / glycoside catabolic process / lysosome
Similarity search - Function
Alpha-L-fucosidase, metazoa-type / Glycoside hydrolase, family 29 / Alpha-L-fucosidase / Alpha-L-fucosidase / Golgi alpha-mannosidase II / Glycosyl hydrolase, all-beta / Glycosidases / Glycoside hydrolase superfamily / TIM Barrel / Alpha-Beta Barrel ...Alpha-L-fucosidase, metazoa-type / Glycoside hydrolase, family 29 / Alpha-L-fucosidase / Alpha-L-fucosidase / Golgi alpha-mannosidase II / Glycosyl hydrolase, all-beta / Glycosidases / Glycoside hydrolase superfamily / TIM Barrel / Alpha-Beta Barrel / Immunoglobulin-like / Sandwich / Mainly Beta / Alpha Beta
Similarity search - Domain/homology
Chem-H76 / IMIDAZOLE / Alpha-L-fucosidase
Similarity search - Component
Biological speciesBacteroides thetaiotaomicron (bacteria)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.1 Å
AuthorsWright, D.W. / Davies, G.J.
CitationJournal: Chembiochem / Year: 2015
Title: Exploiting the Hydrophobic Terrain in Fucosidases with Aryl-Substituted Pyrrolidine Iminosugars.
Authors: Hottin, A. / Wright, D.W. / Davies, G.J. / Behr, J.B.
History
DepositionApr 16, 2014Deposition site: RCSB / Processing site: PDBE
Revision 1.0Jul 2, 2014Provider: repository / Type: Initial release
Revision 1.1Dec 10, 2014Group: Database references
Revision 1.2Jan 21, 2015Group: Database references
Revision 1.3Dec 20, 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 / struct_ncs_dom_lim
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_ncs_dom_lim.beg_auth_comp_id / _struct_ncs_dom_lim.beg_label_asym_id / _struct_ncs_dom_lim.beg_label_comp_id / _struct_ncs_dom_lim.beg_label_seq_id / _struct_ncs_dom_lim.end_auth_comp_id / _struct_ncs_dom_lim.end_label_asym_id / _struct_ncs_dom_lim.end_label_comp_id / _struct_ncs_dom_lim.end_label_seq_id

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Alpha-L-fucosidase
B: Alpha-L-fucosidase
C: Alpha-L-fucosidase
D: Alpha-L-fucosidase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)204,90818
Polymers203,4904
Non-polymers1,41714
Water10,431579
1
A: Alpha-L-fucosidase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)51,2755
Polymers50,8731
Non-polymers4024
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
2
B: Alpha-L-fucosidase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)51,1794
Polymers50,8731
Non-polymers3063
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
3
C: Alpha-L-fucosidase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)51,1794
Polymers50,8731
Non-polymers3063
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
4
D: Alpha-L-fucosidase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)51,2755
Polymers50,8731
Non-polymers4024
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
Unit cell
Length a, b, c (Å)56.610, 188.830, 97.720
Angle α, β, γ (deg.)90.000, 94.300, 90.000
Int Tables number4
Space group name H-MP1211
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11A
21B
12A
22C
13A
23D
14B
24C
15B
25D
16C
26D

NCS domain segments:

Component-ID: 0 / Beg auth comp-ID: GLU / Beg label comp-ID: GLU / Refine code: 0

Dom-IDEns-IDEnd auth comp-IDEnd label comp-IDAuth asym-IDLabel asym-IDAuth seq-IDLabel seq-ID
11ALAALAAA35 - 4711 - 437
21ALAALABB35 - 4711 - 437
12ALAALAAA35 - 4721 - 438
22ALAALACC35 - 4721 - 438
13ARGARGAA35 - 4701 - 436
23ARGARGDD35 - 4701 - 436
14ALAALABB35 - 4711 - 437
24ALAALACC35 - 4711 - 437
15ARGARGBB35 - 4701 - 436
25ARGARGDD35 - 4701 - 436
16ARGARGCC35 - 4701 - 436
26ARGARGDD35 - 4701 - 436

NCS ensembles :
ID
1
2
3
4
5
6

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Components

#1: Protein
Alpha-L-fucosidase /


Mass: 50872.570 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Bacteroides thetaiotaomicron (bacteria)
Strain: ATCC 29148 / DSM 2079 / NCTC 10582 / E50 / VPI-5482 / Gene: BT_2970 / Plasmid: YSBLIC3C / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: Q8A3I4, alpha-L-fucosidase
#2: Chemical
ChemComp-SO4 / SULFATE ION / Sulfate


Mass: 96.063 Da / Num. of mol.: 6 / Source method: obtained synthetically / Formula: SO4
#3: Chemical
ChemComp-IMD / IMIDAZOLE / Imidazole


Mass: 69.085 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C3H5N2
#4: Chemical
ChemComp-H76 / (2S,3S,4R,5S)-2-ethynyl-5-methylpyrrolidine-3,4-diol


Mass: 141.168 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C7H11NO2
#5: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 579 / 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: 2.56 Å3/Da / Density % sol: 51.94 %
Crystal growTemperature: 291.15 K / Method: vapor diffusion, hanging drop
Details: 0.16 M ammonium sulfate, 16% PEG 6000, 0.1 M imidazole

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: Diamond / Beamline: I04-1 / Wavelength: 0.92 Å
DetectorType: DECTRIS PILATUS 2M / Detector: PIXEL / Date: Dec 16, 2012
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.92 Å / Relative weight: 1
ReflectionResolution: 2.1→38.53 Å / Num. obs: 110866 / % possible obs: 93.5 % / Redundancy: 3.6 % / Rmerge(I) obs: 0.119 / Rpim(I) all: 0.068 / Net I/σ(I): 7.2 / Num. measured all: 400515 / Scaling rejects: 219
Reflection shell

Diffraction-ID: 1 / Rejects: 0

Resolution (Å)Redundancy (%)Rmerge(I) obsMean I/σ(I) obsNum. measured allNum. unique allRpim(I) all% possible all
2.1-2.143.60.6841.81872751330.39388.8
11.5-38.534.50.05420.233057330.02897.5

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Processing

Software
NameVersionClassification
iMOSFLM0.1.29data reduction
PDB_EXTRACT3.14data extraction
REFMAC5.8.0069refinement
Aimlessdata scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 2wvv

2wvv


Resolution: 2.1→38.53 Å / Cor.coef. Fo:Fc: 0.944 / Cor.coef. Fo:Fc free: 0.916 / WRfactor Rfree: 0.2311 / WRfactor Rwork: 0.1912 / FOM work R set: 0.7628 / SU B: 7.218 / SU ML: 0.175 / SU R Cruickshank DPI: 0.2565 / SU Rfree: 0.2012 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.256 / ESU R Free: 0.201 / Stereochemistry target values: MAXIMUM LIKELIHOOD
Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. U VALUES REFINED INDIVIDUALLY
RfactorNum. reflection% reflectionSelection details
Rfree0.245 5546 5 %RANDOM
Rwork0.2066 104691 --
obs0.2085 110237 92.82 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK
Displacement parametersBiso max: 137.94 Å2 / Biso mean: 32.203 Å2 / Biso min: 4.72 Å2
Baniso -1Baniso -2Baniso -3
1-2.69 Å20 Å2-1.76 Å2
2--0.01 Å2-0 Å2
3----2.41 Å2
Refinement stepCycle: final / Resolution: 2.1→38.53 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms14026 0 90 579 14695
Biso mean--55.53 28.79 -
Num. residues----1752
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0130.0214569
X-RAY DIFFRACTIONr_bond_other_d0.0070.0213092
X-RAY DIFFRACTIONr_angle_refined_deg1.3991.9319828
X-RAY DIFFRACTIONr_angle_other_deg1.0693.00230087
X-RAY DIFFRACTIONr_dihedral_angle_1_deg5.58251758
X-RAY DIFFRACTIONr_dihedral_angle_2_deg32.33824.023696
X-RAY DIFFRACTIONr_dihedral_angle_3_deg13.675152282
X-RAY DIFFRACTIONr_dihedral_angle_4_deg16.921572
X-RAY DIFFRACTIONr_chiral_restr0.0840.22035
X-RAY DIFFRACTIONr_gen_planes_refined0.0090.02116587
X-RAY DIFFRACTIONr_gen_planes_other0.0060.023525
X-RAY DIFFRACTIONr_mcbond_it2.4593.1777014
X-RAY DIFFRACTIONr_mcbond_other2.4593.1777013
X-RAY DIFFRACTIONr_mcangle_it3.7154.768763
Refine LS restraints NCS

Refine-ID: X-RAY DIFFRACTION / Type: interatomic distance / Weight position: 0.05

Ens-IDDom-IDAuth asym-IDNumberRms dev position (Å)
11A259690.04
12B259690.04
21A259100.05
22C259100.05
31A256990.05
32D256990.05
41B268920.05
42C268920.05
51B264520.05
52D264520.05
61C266180.05
62D266180.05
LS refinement shellResolution: 2.1→2.154 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.347 357 -
Rwork0.295 7004 -
all-7361 -
obs--84.29 %

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