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- PDB-6k8s: Crystal structure of C-domain of baterial malonyl-CoA reductase -

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Basic information

Entry
Database: PDB / ID: 6k8s
TitleCrystal structure of C-domain of baterial malonyl-CoA reductase
ComponentsNAD-dependent epimerase/dehydratase:Short-chain dehydrogenase/reductase SDR
KeywordsOXIDOREDUCTASE / SDR domain
Function / homologyfatty acid elongation / oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor / short chain dehydrogenase / Short-chain dehydrogenase/reductase SDR / NAD(P)-binding domain superfamily / nucleotide binding / NAD-dependent epimerase/dehydratase:Short-chain dehydrogenase/reductase SDR
Function and homology information
Biological speciesPorphyrobacter dokdonensis DSW-74 (bacteria)
MethodX-RAY DIFFRACTION / SYNCHROTRON / SAD / Resolution: 1.8 Å
AuthorsKim, S. / Kim, K.-J.
CitationJournal: Environ.Microbiol. / Year: 2020
Title: Structural insight into bi-functional malonyl-CoA reductase.
Authors: Son, H.F. / Kim, S. / Seo, H. / Hong, J. / Lee, D. / Jin, K.S. / Park, S. / Kim, K.J.
History
DepositionJun 13, 2019Deposition site: PDBJ / Processing site: PDBJ
Revision 1.0Mar 18, 2020Provider: repository / Type: Initial release
Revision 1.1Mar 27, 2024Group: Data collection / Database references / Category: chem_comp_atom / chem_comp_bond / database_2
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: NAD-dependent epimerase/dehydratase:Short-chain dehydrogenase/reductase SDR
B: NAD-dependent epimerase/dehydratase:Short-chain dehydrogenase/reductase SDR
hetero molecules


Theoretical massNumber of molelcules
Total (without water)152,74916
Polymers151,4122
Non-polymers1,33714
Water19,6901093
1


  • Idetical with deposited unit
  • defined by author&software
  • Evidence: gel filtration
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area8780 Å2
ΔGint-182 kcal/mol
Surface area48350 Å2
MethodPISA
Unit cell
Length a, b, c (Å)110.340, 116.687, 134.113
Angle α, β, γ (deg.)90.000, 90.000, 90.000
Int Tables number19
Space group name H-MP212121

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Components

#1: Protein NAD-dependent epimerase/dehydratase:Short-chain dehydrogenase/reductase SDR


Mass: 75705.797 Da / Num. of mol.: 2 / Fragment: SDR C domain
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Porphyrobacter dokdonensis DSW-74 (bacteria)
Gene: I603_0811 / Plasmid: pET28a / Production host: Escherichia coli BL21(DE3) (bacteria) / References: UniProt: A0A1A7BFR5
#2: Chemical ChemComp-GOL / GLYCEROL / GLYCERIN / PROPANE-1,2,3-TRIOL


Mass: 92.094 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C3H8O3 / Feature type: SUBJECT OF INVESTIGATION
#3: Chemical
ChemComp-SO4 / SULFATE ION


Mass: 96.063 Da / Num. of mol.: 12 / Source method: obtained synthetically / Formula: SO4 / Feature type: SUBJECT OF INVESTIGATION
#4: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 1093 / 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: 3.03 Å3/Da / Density % sol: 59.42 %
Crystal growTemperature: 295 K / Method: vapor diffusion, hanging drop / pH: 8 / Details: Li2SO4, HEPES

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: PAL/PLS / Beamline: 7A (6B, 6C1) / Wavelength: 0.97934 Å
DetectorType: ADSC QUANTUM 270 / Detector: CCD / Date: Jul 25, 2018
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.97934 Å / Relative weight: 1
ReflectionResolution: 1.8→50 Å / Num. obs: 156374 / % possible obs: 97.8 % / Redundancy: 5.2 % / CC1/2: 0.996 / Rmerge(I) obs: 0.069 / Rsym value: 0.028 / Net I/σ(I): 31.2
Reflection shellResolution: 1.8→1.83 Å / Rmerge(I) obs: 0.381 / Num. unique obs: 7610 / CC1/2: 0.736 / Rsym value: 0.187

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Phasing

PhasingMethod: SAD

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Processing

Software
NameVersionClassification
HKL-2000data reduction
SOLVEphasing
RESOLVEmodel building
REFMAC5.8.0238refinement
PDB_EXTRACT3.25data extraction
HKL-2000data scaling
RefinementMethod to determine structure: SAD / Resolution: 1.8→29.86 Å / Cor.coef. Fo:Fc: 0.966 / Cor.coef. Fo:Fc free: 0.952 / SU B: 2.307 / SU ML: 0.07 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.1 / ESU R Free: 0.101
Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS U VALUES : REFINED INDIVIDUALLY
RfactorNum. reflection% reflectionSelection details
Rfree0.2042 7789 5 %RANDOM
Rwork0.1737 ---
obs0.1755 148562 97.76 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å
Displacement parametersBiso max: 116.26 Å2 / Biso mean: 26.395 Å2 / Biso min: 8.55 Å2
Baniso -1Baniso -2Baniso -3
1-0.73 Å20 Å2-0 Å2
2---0.38 Å20 Å2
3----0.36 Å2
Refinement stepCycle: final / Resolution: 1.8→29.86 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms10158 0 72 1093 11323
Biso mean--48.65 35.64 -
Num. residues----1324
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0120.01310483
X-RAY DIFFRACTIONr_bond_other_d0.0010.0179822
X-RAY DIFFRACTIONr_angle_refined_deg1.6731.63914240
X-RAY DIFFRACTIONr_angle_other_deg1.4561.57522653
X-RAY DIFFRACTIONr_dihedral_angle_1_deg6.59551340
X-RAY DIFFRACTIONr_dihedral_angle_2_deg33.44521.149583
X-RAY DIFFRACTIONr_dihedral_angle_3_deg14.04151727
X-RAY DIFFRACTIONr_dihedral_angle_4_deg17.41915100
X-RAY DIFFRACTIONr_chiral_restr0.0840.21349
X-RAY DIFFRACTIONr_gen_planes_refined0.0090.0211972
X-RAY DIFFRACTIONr_gen_planes_other0.0010.022268
LS refinement shellResolution: 1.801→1.848 Å / Rfactor Rfree error: 0 / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.255 540 -
Rwork0.248 10627 -
all-11167 -
obs--95.17 %

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