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- PDB-4jf1: R144Q mutant of N-acetylornithine aminotransferase -

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Basic information

Entry
Database: PDB / ID: 4jf1
TitleR144Q mutant of N-acetylornithine aminotransferase
ComponentsAcetylornithine/succinyldiaminopimelate aminotransferase
KeywordsTRANSFERASE / PLP dependent fold type I sub class II aminotransferase
Function / homology
Function and homology information


succinyldiaminopimelate transaminase / succinyldiaminopimelate transaminase activity / acetylornithine transaminase / N2-acetyl-L-ornithine:2-oxoglutarate 5-aminotransferase activity / L-arginine biosynthetic process / lysine biosynthetic process via diaminopimelate / pyridoxal phosphate binding / identical protein binding / cytoplasm
Similarity search - Function
Acetyl/Succinylornithine transaminase family, bacteria / Acetylornithine/Succinylornithine transaminase family / : / : / Aminotransferases class-III pyridoxal-phosphate attachment site. / Aminotransferase class-III / Aminotransferase class-III / Aspartate Aminotransferase, domain 1 / Aspartate Aminotransferase, domain 1 / Aspartate Aminotransferase; domain 2 ...Acetyl/Succinylornithine transaminase family, bacteria / Acetylornithine/Succinylornithine transaminase family / : / : / Aminotransferases class-III pyridoxal-phosphate attachment site. / Aminotransferase class-III / Aminotransferase class-III / Aspartate Aminotransferase, domain 1 / Aspartate Aminotransferase, domain 1 / Aspartate Aminotransferase; domain 2 / Type I PLP-dependent aspartate aminotransferase-like (Major domain) / Pyridoxal phosphate-dependent transferase, small domain / Pyridoxal phosphate-dependent transferase, major domain / Pyridoxal phosphate-dependent transferase / Alpha-Beta Complex / 3-Layer(aba) Sandwich / Alpha Beta
Similarity search - Domain/homology
ACETATE ION / PYRIDOXAL-5'-PHOSPHATE / Acetylornithine/succinyldiaminopimelate aminotransferase
Similarity search - Component
Biological speciesSalmonella typhimurium (bacteria)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.28 Å
AuthorsBisht, S. / Bharath, S.R. / Murthy, M.R.N.
CitationJournal: To be Published
Title: Conformational transitions, ligand specificity and catalysis in N-acetylornithine aminotransferase: Implications on drug designing and rational enzyme engineering in omega aminotransferases
Authors: Bisht, S. / Bharath, S.R. / Murthy, M.R.N.
History
DepositionFeb 27, 2013Deposition site: RCSB / Processing site: PDBJ
Revision 1.0Mar 26, 2014Provider: 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

Downloads & links

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Assembly

Deposited unit
A: Acetylornithine/succinyldiaminopimelate aminotransferase
B: Acetylornithine/succinyldiaminopimelate aminotransferase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)92,46113
Polymers91,4202
Non-polymers1,04111
Water13,313739
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area10360 Å2
ΔGint-49 kcal/mol
Surface area25110 Å2
MethodPISA
Unit cell
Length a, b, c (Å)97.080, 112.000, 65.320
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-601-

HOH

21B-860-

HOH

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Components

#1: Protein Acetylornithine/succinyldiaminopimelate aminotransferase / ACOAT / DapATase / Succinyldiaminopimelate transferase


Mass: 45709.891 Da / Num. of mol.: 2 / Mutation: R144Q, A298T
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Salmonella typhimurium (bacteria) / Strain: LT2 / Gene: argD, dapC, dtu, STM3468 / Plasmid: pRSET C / Production host: Escherichia coli (E. coli) / Strain (production host): BL21 (DE3) Rosetta
References: UniProt: P40732, acetylornithine transaminase, succinyldiaminopimelate transaminase
#2: Chemical ChemComp-PLP / PYRIDOXAL-5'-PHOSPHATE / VITAMIN B6 Phosphate


Mass: 247.142 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C8H10NO6P
#3: Chemical
ChemComp-EDO / 1,2-ETHANEDIOL / ETHYLENE GLYCOL


Mass: 62.068 Da / Num. of mol.: 5 / Source method: obtained synthetically / Formula: C2H6O2
#4: Chemical
ChemComp-ACT / ACETATE ION


Mass: 59.044 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C2H3O2
#5: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 739 / 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: 1.94 Å3/Da / Density % sol: 36.67 %
Crystal growTemperature: 295 K / Method: vapor diffusion, hanging drop / pH: 8.5
Details: 20% PEG 3350, 0.5M ammonium acetate, 0.1M Tris pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 295K

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: ESRF / Beamline: BM14 / Wavelength: 0.9537 Å
DetectorType: MARMOSAIC 225 mm CCD / Detector: CCD / Date: Jul 18, 2012 / Details: Bent collimating mirror and toroid
RadiationMonochromator: Si(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9537 Å / Relative weight: 1
ReflectionResolution: 1.28→112 Å / Num. obs: 178148 / % possible obs: 98.3 % / Redundancy: 4.7 % / Biso Wilson estimate: 9.1 Å2 / Rmerge(I) obs: 0.06 / Net I/σ(I): 14.1
Reflection shell
Resolution (Å)Redundancy (%)Rmerge(I) obsMean I/σ(I) obsNum. unique allDiffraction-ID% possible all
1.28-1.354.30.463.224842195
4.06-22.754.90.0239.76061199

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Processing

Software
NameVersionClassification
HKL-2000data collection
PHASERphasing
REFMAC5.6.0117refinement
MOSFLMdata reduction
SCALAdata scaling
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 2PB0

2pb0


Resolution: 1.28→22.75 Å / Cor.coef. Fo:Fc: 0.966 / Cor.coef. Fo:Fc free: 0.961 / SU B: 0.631 / SU ML: 0.028 / Cross valid method: THROUGHOUT / ESU R: 0.048 / ESU R Free: 0.048 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN USED IF PRESENT IN THE INPUT
RfactorNum. reflection% reflectionSelection details
Rfree0.18006 8916 5 %RANDOM
Rwork0.16758 ---
obs0.16821 169162 98.13 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK
Displacement parametersBiso mean: 11.265 Å2
Baniso -1Baniso -2Baniso -3
1--0.13 Å20 Å20 Å2
2---0.04 Å20 Å2
3---0.17 Å2
Refinement stepCycle: LAST / Resolution: 1.28→22.75 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms5862 0 66 739 6667
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0070.026235
X-RAY DIFFRACTIONr_angle_refined_deg1.2721.9518470
X-RAY DIFFRACTIONr_dihedral_angle_1_deg5.7145813
X-RAY DIFFRACTIONr_dihedral_angle_2_deg33.39824.27274
X-RAY DIFFRACTIONr_dihedral_angle_3_deg11.64615960
X-RAY DIFFRACTIONr_dihedral_angle_4_deg17.6461526
X-RAY DIFFRACTIONr_chiral_restr0.0810.2930
X-RAY DIFFRACTIONr_gen_planes_refined0.0070.0214824
LS refinement shellResolution: 1.284→1.317 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.233 568 -
Rwork0.241 11521 -
obs--94.23 %

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