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- PDB-3wjy: Orotidine 5'-monophosphate decarboxylase K72A mutant from M. ther... -

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Basic information

Entry
Database: PDB / ID: 3wjy
TitleOrotidine 5'-monophosphate decarboxylase K72A mutant from M. thermoautotrophicus complexed with 6-amino-UMP
ComponentsOrotidine 5'-phosphate decarboxylase
KeywordsLYASE / protein-ligand complex / TIM barrel / decarboxylase / pyrimidine biosynthesis
Function / homology
Function and homology information


orotidine-5'-phosphate decarboxylase / orotidine-5'-phosphate decarboxylase activity / 'de novo' UMP biosynthetic process / 'de novo' pyrimidine nucleobase biosynthetic process
Similarity search - Function
: / Orotidine 5'-phosphate decarboxylase / Orotidine 5'-phosphate decarboxylase, active site / Orotidine 5'-phosphate decarboxylase active site. / Orotidine 5'-phosphate decarboxylase domain / Orotidine 5'-phosphate decarboxylase / HUMPS family / Orotidine 5'-phosphate decarboxylase / HUMPS family / Ribulose-phosphate binding barrel / Aldolase class I / Aldolase-type TIM barrel ...: / Orotidine 5'-phosphate decarboxylase / Orotidine 5'-phosphate decarboxylase, active site / Orotidine 5'-phosphate decarboxylase active site. / Orotidine 5'-phosphate decarboxylase domain / Orotidine 5'-phosphate decarboxylase / HUMPS family / Orotidine 5'-phosphate decarboxylase / HUMPS family / Ribulose-phosphate binding barrel / Aldolase class I / Aldolase-type TIM barrel / TIM Barrel / Alpha-Beta Barrel / Alpha Beta
Similarity search - Domain/homology
6-AMINOURIDINE 5'-MONOPHOSPHATE / Orotidine 5'-phosphate decarboxylase
Similarity search - Component
Biological speciesMethanothermobacter thermautotrophicus (archaea)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.72 Å
AuthorsFujihashi, M. / Pai, E.F. / Miki, K.
CitationJournal: J.Am.Chem.Soc. / Year: 2013
Title: Substrate distortion contributes to the catalysis of orotidine 5'-monophosphate decarboxylase.
Authors: Fujihashi, M. / Ishida, T. / Kuroda, S. / Kotra, L.P. / Pai, E.F. / Miki, K.
History
DepositionOct 17, 2013Deposition site: PDBJ / Processing site: PDBJ
Revision 1.0Dec 4, 2013Provider: repository / Type: Initial release
Revision 1.1Nov 8, 2023Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model / pdbx_struct_special_symmetry / struct_ref_seq_dif / struct_site
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_ref_seq_dif.details / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: Orotidine 5'-phosphate decarboxylase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)27,7533
Polymers27,3211
Non-polymers4312
Water2,450136
1
A: Orotidine 5'-phosphate decarboxylase
hetero molecules

A: Orotidine 5'-phosphate decarboxylase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)55,5056
Polymers54,6432
Non-polymers8634
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation4_566x,-y+1,-z+11
Buried area5070 Å2
ΔGint-45 kcal/mol
Surface area15330 Å2
MethodPISA
Unit cell
Length a, b, c (Å)58.118, 103.527, 74.046
Angle α, β, γ (deg.)90.000, 90.000, 90.000
Int Tables number20
Space group name H-MC2221
Components on special symmetry positions
IDModelComponents
11A-100-

PHE

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Components

#1: Protein Orotidine 5'-phosphate decarboxylase / / OMP decarboxylase / OMPDCase / OMPdecase


Mass: 27321.299 Da / Num. of mol.: 1 / Mutation: K72A, L226R, N227I
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Methanothermobacter thermautotrophicus (archaea)
Strain: ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H
Gene: pyrF, MTH_129 / Plasmid: pET15b / Production host: Escherichia coli (E. coli)
References: UniProt: O26232, orotidine-5'-phosphate decarboxylase
#2: Chemical ChemComp-NUP / 6-AMINOURIDINE 5'-MONOPHOSPHATE


Mass: 339.196 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C9H14N3O9P
#3: Chemical ChemComp-GOL / GLYCEROL / GLYCERIN / PROPANE-1,2,3-TRIOL / Glycerol


Mass: 92.094 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C3H8O3
#4: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 136 / Source method: isolated from a natural source / Formula: H2O
Sequence detailsACCORDING TO DEPOSITORS, PRO101 IS CORRECT AND UNIPORT IS PROBABLY INCORRECT AT THIS POSITION. ...ACCORDING TO DEPOSITORS, PRO101 IS CORRECT AND UNIPORT IS PROBABLY INCORRECT AT THIS POSITION. DEPOSITORS SEQUENCED THE GENOME FROM M. THERMOAUTOTROPHICUS AND CONFIRMED IT IS PRO.

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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: 2.04 Å3/Da / Density % sol: 39.66 %
Crystal growTemperature: 293 K / Method: vapor diffusion / pH: 6.5
Details: Sodium citrate, pH 6.5, VAPOR DIFFUSION, temperature 293K

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 14-BM-C / Wavelength: 0.9 Å
DetectorType: ADSC QUANTUM 315 / Detector: CCD
RadiationMonochromator: Default / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9 Å / Relative weight: 1
ReflectionResolution: 1.72→51.78 Å / Num. obs: 24073 / % possible obs: 99.9 % / Rmerge(I) obs: 0.058 / Net I/σ(I): 34.8
Reflection shellResolution: 1.72→1.76 Å / Rmerge(I) obs: 0.315 / % possible all: 100

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Processing

Software
NameVersionClassificationNB
REFMAC5.5.0102refinement
PDB_EXTRACT3.11data extraction
HKL-2000data collection
HKL-2000data reduction
HKL-2000data scaling
MOLREPphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 1DVJ

1dvj


Resolution: 1.72→50 Å / Cor.coef. Fo:Fc: 0.969 / Cor.coef. Fo:Fc free: 0.96 / Occupancy max: 1 / Occupancy min: 0.3 / SU B: 3.506 / SU ML: 0.053 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.092 / ESU R Free: 0.091 / Stereochemistry target values: MAXIMUM LIKELIHOOD
RfactorNum. reflection% reflectionSelection details
Rfree0.1811 1204 5 %RANDOM
Rwork0.1494 ---
obs0.151 24045 99.76 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK
Displacement parametersBiso max: 67.67 Å2 / Biso mean: 19.5217 Å2 / Biso min: 5.58 Å2
Baniso -1Baniso -2Baniso -3
1-0.32 Å20 Å20 Å2
2---0.73 Å20 Å2
3---0.41 Å2
Refinement stepCycle: LAST / Resolution: 1.72→50 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms1626 0 28 136 1790
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0190.0221785
X-RAY DIFFRACTIONr_angle_refined_deg1.7291.9942429
X-RAY DIFFRACTIONr_dihedral_angle_1_deg5.8335237
X-RAY DIFFRACTIONr_dihedral_angle_2_deg38.57423.33378
X-RAY DIFFRACTIONr_dihedral_angle_3_deg13.69515302
X-RAY DIFFRACTIONr_dihedral_angle_4_deg20.1891518
X-RAY DIFFRACTIONr_chiral_restr0.1320.2274
X-RAY DIFFRACTIONr_gen_planes_refined0.0120.0221373
X-RAY DIFFRACTIONr_mcbond_it1.1231.51131
X-RAY DIFFRACTIONr_mcangle_it2.00421828
X-RAY DIFFRACTIONr_scbond_it3.4013654
X-RAY DIFFRACTIONr_scangle_it5.884.5600
LS refinement shellResolution: 1.72→1.765 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.264 80 -
Rwork0.18 1634 -
all-1714 -
obs--97.94 %
Refinement TLS params.Method: refined / Origin x: 18.5892 Å / Origin y: 40.45 Å / Origin z: 29.9529 Å
111213212223313233
T0.021 Å20.0017 Å2-0.0038 Å2-0.0135 Å20.0003 Å2--0.0063 Å2
L0.3405 °2-0.0273 °20.0053 °2-0.5603 °2-0.0171 °2--0.2146 °2
S-0.0001 Å °0.0237 Å °-0.0355 Å °-0.0665 Å °0.0128 Å °0.0021 Å °0.0274 Å °0.0069 Å °-0.0127 Å °
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1A11 - 225
2X-RAY DIFFRACTION1A301
3X-RAY DIFFRACTION1A302
4X-RAY DIFFRACTION1A401 - 536

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