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- PDB-6zlk: Equilibrium Structure of UDP-Glucuronic acid 4-epimerase from Bac... -

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Basic information

Entry
Database: PDB / ID: 6zlk
TitleEquilibrium Structure of UDP-Glucuronic acid 4-epimerase from Bacillus cereus in complex with UDP-Glucuronic acid/UDP-Galacturonic acid and NAD
ComponentsEpimerase domain-containing protein
KeywordsOXIDOREDUCTASE / epimerase / UDP-Glucuronic acid / UDP-Galacturonic acid / equilibrium / NAD / UDP-sugar binding protein
Function / homologyNAD-dependent epimerase/dehydratase / NAD dependent epimerase/dehydratase family / catalytic activity / NAD(P)-binding domain superfamily / NICOTINAMIDE-ADENINE-DINUCLEOTIDE / URIDINE-5'-DIPHOSPHATE-GLUCURONIC ACID / Chem-UGB / Epimerase domain-containing protein
Function and homology information
Biological speciesBacillus cereus HuA2-4 (bacteria)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.5 Å
AuthorsIacovino, L.G. / Mattevi, A.
Funding support Italy, 1items
OrganizationGrant numberCountry
Italian Ministry of Education Italy
CitationJournal: J.Biol.Chem. / Year: 2020
Title: Crystallographic snapshots of UDP-glucuronic acid 4-epimerase ligand binding, rotation, and reduction.
Authors: Iacovino, L.G. / Savino, S. / Borg, A.J.E. / Binda, C. / Nidetzky, B. / Mattevi, A.
History
DepositionJun 30, 2020Deposition site: PDBE / Processing site: PDBE
Revision 1.0Jul 29, 2020Provider: repository / Type: Initial release
Revision 1.1Sep 9, 2020Group: Database references / Category: citation / citation_author
Item: _citation.journal_volume / _citation.page_first ..._citation.journal_volume / _citation.page_first / _citation.page_last / _citation.title / _citation_author.identifier_ORCID
Revision 1.2Jan 31, 2024Group: 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: Epimerase domain-containing protein
B: Epimerase domain-containing protein
C: Epimerase domain-containing protein
D: Epimerase domain-containing protein
hetero molecules


Theoretical massNumber of molelcules
Total (without water)153,40416
Polymers146,1084
Non-polymers7,29612
Water16,826934
1
A: Epimerase domain-containing protein
C: Epimerase domain-containing protein
hetero molecules


Theoretical massNumber of molelcules
Total (without water)76,7028
Polymers73,0542
Non-polymers3,6486
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area6180 Å2
ΔGint-54 kcal/mol
Surface area23250 Å2
MethodPISA
2
B: Epimerase domain-containing protein
D: Epimerase domain-containing protein
hetero molecules


Theoretical massNumber of molelcules
Total (without water)76,7028
Polymers73,0542
Non-polymers3,6486
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area6360 Å2
ΔGint-51 kcal/mol
Surface area23570 Å2
MethodPISA
Unit cell
Length a, b, c (Å)53.737, 124.349, 98.364
Angle α, β, γ (deg.)90.000, 90.630, 90.000
Int Tables number4
Space group name H-MP1211

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Components

#1: Protein
Epimerase domain-containing protein


Mass: 36526.957 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Bacillus cereus HuA2-4 (bacteria) / Gene: IG7_05634 / Production host: Escherichia coli (E. coli) / References: UniProt: J8BY31
#2: Chemical
ChemComp-NAD / NICOTINAMIDE-ADENINE-DINUCLEOTIDE


Mass: 663.425 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C21H27N7O14P2 / Feature type: SUBJECT OF INVESTIGATION / Comment: NAD*YM
#3: Chemical
ChemComp-UGA / URIDINE-5'-DIPHOSPHATE-GLUCURONIC ACID / UDP-GLUCURONIC ACID


Mass: 580.285 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C15H22N2O18P2 / Feature type: SUBJECT OF INVESTIGATION
#4: Chemical
ChemComp-UGB / (2S,3R,4S,5R,6R)-6-[[[(2R,3S,4R,5R)-5-(2,4-dioxopyrimidin-1-yl)-3,4-dihydroxy-oxolan-2-yl]methoxy-hydroxy-phosphoryl]oxy-hydroxy-phosphoryl]oxy-3,4,5-trihydroxy-oxane-2-carboxylic acid


Mass: 580.285 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C15H22N2O18P2 / Feature type: SUBJECT OF INVESTIGATION
#5: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 934 / Source method: isolated from a natural source / Formula: H2O
Has ligand of interestY

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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: 2.25 Å3/Da / Density % sol: 45.31 %
Crystal growTemperature: 277 K / Method: vapor diffusion / pH: 7 / Details: 200 mM potassium acetate, 14-24% PEG3350

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: SLS / Beamline: X06SA / Wavelength: 0.98 Å
DetectorType: DECTRIS EIGER X 16M / Detector: PIXEL / Date: Mar 29, 2019
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.98 Å / Relative weight: 1
ReflectionResolution: 1.5→49.37 Å / Num. obs: 190286 / % possible obs: 97 % / Redundancy: 3.8 % / CC1/2: 0.99 / Net I/σ(I): 7
Reflection shellResolution: 1.5→1.53 Å / Num. unique obs: 14125 / CC1/2: 0.3

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Processing

Software
NameVersionClassification
REFMAC5.8.0238refinement
PDB_EXTRACT3.25data extraction
XDSdata reduction
Aimlessdata scaling
MOLREPphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 5U4Q

5u4q


Resolution: 1.5→49.37 Å / Cor.coef. Fo:Fc: 0.975 / Cor.coef. Fo:Fc free: 0.965 / SU B: 1.922 / SU ML: 0.066 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.074 / ESU R Free: 0.076 / Stereochemistry target values: MAXIMUM LIKELIHOOD
Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS U VALUES : REFINED INDIVIDUALLY
RfactorNum. reflection% reflectionSelection details
Rfree0.2035 10018 5 %RANDOM
Rwork0.1721 ---
obs0.1736 190286 97.34 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK
Displacement parametersBiso max: 128.99 Å2 / Biso mean: 23.947 Å2 / Biso min: 9.05 Å2
Baniso -1Baniso -2Baniso -3
1--0.65 Å20 Å20.5 Å2
2--0.68 Å20 Å2
3----0.04 Å2
Refinement stepCycle: final / Resolution: 1.5→49.37 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms9867 0 472 934 11273
Biso mean--23.88 38.22 -
Num. residues----1260
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0120.01310587
X-RAY DIFFRACTIONr_bond_other_d0.0010.0179739
X-RAY DIFFRACTIONr_angle_refined_deg1.7221.65114438
X-RAY DIFFRACTIONr_angle_other_deg1.4811.57422718
X-RAY DIFFRACTIONr_dihedral_angle_1_deg6.82351255
X-RAY DIFFRACTIONr_dihedral_angle_2_deg36.07323.318449
X-RAY DIFFRACTIONr_dihedral_angle_3_deg12.983151796
X-RAY DIFFRACTIONr_dihedral_angle_4_deg14.0161537
X-RAY DIFFRACTIONr_chiral_restr0.0870.21504
X-RAY DIFFRACTIONr_gen_planes_refined0.010.0211319
X-RAY DIFFRACTIONr_gen_planes_other0.0010.022016
LS refinement shellResolution: 1.5→1.539 Å / Rfactor Rfree error: 0 / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.309 728 -
Rwork0.322 14125 -
all-14853 -
obs--97.34 %

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