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- PDB-3td6: Peptidyl-tRNA hydrolase from Mycobacterium tuberculosis from trig... -

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Basic information

Entry
Database: PDB / ID: 3td6
TitlePeptidyl-tRNA hydrolase from Mycobacterium tuberculosis from trigonal partially dehydrated crystal
ComponentsPeptidyl-tRNA hydrolase
KeywordsHYDROLASE / Pth / Hydrolysis of Peptidyl-tRNA / Peptidyl-tRNA / Cytosol
Function / homology
Function and homology information


peptidyl-tRNA hydrolase / aminoacyl-tRNA hydrolase activity / translation / plasma membrane / cytoplasm
Similarity search - Function
Peptidyl-tRNA hydrolase / Peptidyl-tRNA hydrolase signature 2. / Peptidyl-tRNA hydrolase signature 1. / Peptidyl-tRNA hydrolase / Peptidyl-tRNA hydrolase, conserved site / Peptidyl-tRNA hydrolase superfamily / Peptidyl-tRNA hydrolase / Rossmann fold / 3-Layer(aba) Sandwich / Alpha Beta
Similarity search - Domain/homology
Peptidyl-tRNA hydrolase / Peptidyl-tRNA hydrolase
Similarity search - Component
Biological speciesMycobacterium tuberculosis (bacteria)
MethodX-RAY DIFFRACTION / MOLECULAR REPLACEMENT / Resolution: 3.2 Å
AuthorsSelvaraj, M. / Ahmad, R. / Varshney, U. / Vijayan, M.
CitationJournal: Acta Crystallogr.,Sect.F / Year: 2012
Title: Structures of new crystal forms of Mycobacterium tuberculosis peptidyl-tRNA hydrolase and functionally important plasticity of the molecule
Authors: Selvaraj, M. / Ahmad, R. / Varshney, U. / Vijayan, M.
History
DepositionAug 10, 2011Deposition site: RCSB / Processing site: PDBJ
Revision 1.0Feb 15, 2012Provider: repository / Type: Initial release
Revision 1.1Nov 1, 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

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Assembly

Deposited unit
A: Peptidyl-tRNA hydrolase


Theoretical massNumber of molelcules
Total (without water)20,4861
Polymers20,4861
Non-polymers00
Water32418
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
Unit cell
Length a, b, c (Å)59.470, 59.470, 80.420
Angle α, β, γ (deg.)90.00, 90.00, 120.00
Int Tables number154
Space group name H-MP3221

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Components

#1: Protein Peptidyl-tRNA hydrolase / PTH


Mass: 20485.531 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Mycobacterium tuberculosis (bacteria) / Strain: H37Rv / Gene: MT1042, MTCY10G2.35, pth, Rv1014c / Plasmid: pRSETBMtuPth / Production host: Escherichia coli (E. coli) / Strain (production host): BL21
References: UniProt: P65865, UniProt: P9WHN7*PLUS, peptidyl-tRNA hydrolase
#2: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 18 / 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 Å3/Da / Density % sol: 38.62 %
Crystal growTemperature: 291 K / Method: microbatch under oil / pH: 7.5
Details: 0.1M HEPES, 25% PEG 8000, 5% dioxane, pH 7.5, Microbatch under oil, temperature 291K

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: ROTATING ANODE / Type: RIGAKU MICROMAX-007 HF / Wavelength: 1.54 Å
DetectorType: MAR scanner 345 mm plate / Detector: IMAGE PLATE / Date: Jun 8, 2010 / Details: Mirrors
RadiationMonochromator: Osmic mirror / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.54 Å / Relative weight: 1
ReflectionResolution: 3.2→43 Å / Num. obs: 2900 / Redundancy: 3.9 % / Biso Wilson estimate: 32.3 Å2 / Rmerge(I) obs: 0.155 / Net I/σ(I): 9.9
Reflection shellResolution: 3.2→3.37 Å

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Processing

Software
NameVersionClassification
MAR345dtbdata collection
PHASERphasing
REFMAC5.2.0019refinement
MOSFLMdata reduction
SCALAdata scaling
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB ENTRY 2Z2I

2z2i


Resolution: 3.2→30 Å / Cor.coef. Fo:Fc: 0.878 / Cor.coef. Fo:Fc free: 0.834 / SU B: 47.347 / SU ML: 0.393 / Cross valid method: THROUGHOUT / ESU R Free: 0.62 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
RfactorNum. reflection% reflectionSelection details
Rfree0.2698 132 4.6 %RANDOM
Rwork0.23172 ---
obs0.23347 2750 98.36 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: BABINET MODEL WITH MASK
Displacement parametersBiso mean: 18.918 Å2
Baniso -1Baniso -2Baniso -3
1--1.8 Å2-0.9 Å20 Å2
2---1.8 Å20 Å2
3---2.7 Å2
Refinement stepCycle: LAST / Resolution: 3.2→30 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms1340 0 0 18 1358
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0130.0221363
X-RAY DIFFRACTIONr_angle_refined_deg1.5261.9751846
X-RAY DIFFRACTIONr_dihedral_angle_1_deg4.6795183
X-RAY DIFFRACTIONr_dihedral_angle_2_deg40.16122.72755
X-RAY DIFFRACTIONr_dihedral_angle_3_deg22.10615211
X-RAY DIFFRACTIONr_dihedral_angle_4_deg19.9921513
X-RAY DIFFRACTIONr_chiral_restr0.0930.2208
X-RAY DIFFRACTIONr_gen_planes_refined0.0080.021050
X-RAY DIFFRACTIONr_nbd_refined0.2850.2640
X-RAY DIFFRACTIONr_nbtor_refined0.3270.2892
X-RAY DIFFRACTIONr_xyhbond_nbd_refined0.2090.258
X-RAY DIFFRACTIONr_symmetry_vdw_refined0.330.235
X-RAY DIFFRACTIONr_symmetry_hbond_refined0.3720.22
X-RAY DIFFRACTIONr_mcbond_it11.6821.5923
X-RAY DIFFRACTIONr_mcangle_it15.65121429
X-RAY DIFFRACTIONr_scbond_it0.4353474
X-RAY DIFFRACTIONr_scangle_it0.4894.5417
LS refinement shellResolution: 3.2→3.282 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.182 7 -
Rwork0.234 197 -
obs--100 %
Refinement TLS params.Method: refined / Origin x: 14.3654 Å / Origin y: -20.7885 Å / Origin z: 8.3273 Å
111213212223313233
T0.0636 Å2-0.0041 Å2-0.0077 Å2-0.0781 Å20.0318 Å2--0.0382 Å2
L0.9973 °20.0185 °20.0578 °2-0.6843 °20.3048 °2--0.3718 °2
S0.0936 Å °-0.02 Å °0.0083 Å °0.0682 Å °-0.0498 Å °-0.0437 Å °0.0102 Å °-0.004 Å °-0.0439 Å °

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