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- PDB-8zw1: citrate synthases complexed with oxaloacetate and acetyl-CoA -

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Basic information

Entry
Database: PDB / ID: 8zw1
Titlecitrate synthases complexed with oxaloacetate and acetyl-CoA
ComponentsCitrate synthase, mitochondrial
KeywordsTRANSFERASE / citrate synthase / complex
Function / homology
Function and homology information


citrate (Si)-synthase / : / Citric acid cycle (TCA cycle) / citrate metabolic process / Maturation of TCA enzymes and regulation of TCA cycle / Mitochondrial protein import / tricarboxylic acid cycle / Mitochondrial protein degradation / carbohydrate metabolic process / mitochondrial matrix ...citrate (Si)-synthase / : / Citric acid cycle (TCA cycle) / citrate metabolic process / Maturation of TCA enzymes and regulation of TCA cycle / Mitochondrial protein import / tricarboxylic acid cycle / Mitochondrial protein degradation / carbohydrate metabolic process / mitochondrial matrix / mitochondrion / RNA binding / extracellular exosome / identical protein binding / nucleus
Similarity search - Function
Citrate synthase, eukaryotic-type / Citrate synthase active site / Citrate synthase signature. / Citrate synthase-like, large alpha subdomain / Citrate synthase / Citrate synthase-like, small alpha subdomain / Citrate synthase superfamily / Citrate synthase, C-terminal domain
Similarity search - Domain/homology
ACETYL COENZYME *A / CITRIC ACID / COENZYME A / OXALOACETATE ION / Citrate synthase, mitochondrial
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.1 Å
AuthorsYang, L.Y. / Fang, Y.J.
Funding support China, 1items
OrganizationGrant numberCountry
National Natural Science Foundation of China (NSFC) China
CitationJournal: To Be Published
Title: citrate synthases complexed with oxaloacetate and acetyl-CoA
Authors: Yang, L.Y. / Fang, Y.J.
History
DepositionJun 12, 2024Deposition site: PDBJ / Processing site: PDBJ
Revision 1.0Jun 18, 2025Provider: repository / Type: Initial release

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: Citrate synthase, mitochondrial
B: Citrate synthase, mitochondrial
hetero molecules


Theoretical massNumber of molelcules
Total (without water)99,1656
Polymers97,2652
Non-polymers1,9004
Water2,558142
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area12110 Å2
ΔGint-53 kcal/mol
Surface area29520 Å2
MethodPISA
Unit cell
Length a, b, c (Å)57.523, 59.789, 72.582
Angle α, β, γ (deg.)102.52, 98.23, 118.76
Int Tables number1
Space group name H-MP1

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Components

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Protein , 1 types, 2 molecules AB

#1: Protein Citrate synthase, mitochondrial / Citrate (Si)-synthase


Mass: 48632.547 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: CS / Production host: Escherichia coli (E. coli) / References: UniProt: O75390, citrate (Si)-synthase

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Non-polymers , 5 types, 146 molecules

#2: Chemical ChemComp-COA / COENZYME A


Mass: 767.534 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C21H36N7O16P3S
#3: Chemical ChemComp-CIT / CITRIC ACID


Mass: 192.124 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C6H8O7
#4: Chemical ChemComp-OAA / OXALOACETATE ION


Mass: 131.064 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C4H3O5
#5: Chemical ChemComp-ACO / ACETYL COENZYME *A


Mass: 809.571 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C23H38N7O17P3S
#6: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 142 / Source method: isolated from a natural source / Formula: H2O

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Details

Has ligand of interestN
Has protein modificationN

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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: 2.1 Å3/Da / Density % sol: 41.5 %
Crystal growTemperature: 289.15 K / Method: vapor diffusion, sitting drop / Details: 0.2 M ammonium acetate pH=7.1, 20% w/v PEG3350

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: SSRF / Beamline: BL10U2 / Wavelength: 0.979 Å
DetectorType: DECTRIS EIGER X 16M / Detector: PIXEL / Date: Oct 26, 2023
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.979 Å / Relative weight: 1
ReflectionResolution: 2.03→67.83 Å / Num. obs: 48136 / % possible obs: 94.2 % / Redundancy: 2 % / CC1/2: 0.978 / Rmerge(I) obs: 0.114 / Rrim(I) all: 0.151 / Net I/σ(I): 1.6
Reflection shellResolution: 2.03→2.14 Å / Rmerge(I) obs: 0.841 / Num. unique obs: 7190 / CC1/2: 0.223 / Rrim(I) all: 1.134

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Processing

Software
NameVersionClassification
REFMAC5.8.0419refinement
XDSdata reduction
XDSdata scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT / Resolution: 2.1→41.12 Å / Cor.coef. Fo:Fc: 0.94 / Cor.coef. Fo:Fc free: 0.894 / SU B: 16.362 / SU ML: 0.409 / Cross valid method: THROUGHOUT / ESU R: 0.374 / ESU R Free: 0.269 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
RfactorNum. reflection% reflectionSelection details
Rfree0.29869 2024 4.7 %RANDOM
Rwork0.23298 ---
obs0.23601 41416 93.89 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK
Displacement parametersBiso mean: 48.895 Å2
Baniso -1Baniso -2Baniso -3
1--0 Å2-0.01 Å20 Å2
2---0 Å20.01 Å2
3---0 Å2
Refinement stepCycle: 1 / Resolution: 2.1→41.12 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms6813 0 121 142 7076
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0030.0127114
X-RAY DIFFRACTIONr_bond_other_d0.0010.0166637
X-RAY DIFFRACTIONr_angle_refined_deg1.1181.8279683
X-RAY DIFFRACTIONr_angle_other_deg0.3981.74315285
X-RAY DIFFRACTIONr_dihedral_angle_1_deg6.2015870
X-RAY DIFFRACTIONr_dihedral_angle_2_deg6.495543
X-RAY DIFFRACTIONr_dihedral_angle_3_deg13.539101163
X-RAY DIFFRACTIONr_dihedral_angle_4_deg
X-RAY DIFFRACTIONr_chiral_restr0.0540.21067
X-RAY DIFFRACTIONr_gen_planes_refined0.0040.028333
X-RAY DIFFRACTIONr_gen_planes_other0.0010.021613
X-RAY DIFFRACTIONr_nbd_refined
X-RAY DIFFRACTIONr_nbd_other
X-RAY DIFFRACTIONr_nbtor_refined
X-RAY DIFFRACTIONr_nbtor_other
X-RAY DIFFRACTIONr_xyhbond_nbd_refined
X-RAY DIFFRACTIONr_xyhbond_nbd_other
X-RAY DIFFRACTIONr_metal_ion_refined
X-RAY DIFFRACTIONr_metal_ion_other
X-RAY DIFFRACTIONr_symmetry_vdw_refined
X-RAY DIFFRACTIONr_symmetry_vdw_other
X-RAY DIFFRACTIONr_symmetry_hbond_refined
X-RAY DIFFRACTIONr_symmetry_hbond_other
X-RAY DIFFRACTIONr_symmetry_metal_ion_refined
X-RAY DIFFRACTIONr_symmetry_metal_ion_other
X-RAY DIFFRACTIONr_mcbond_it2.5644.8963475
X-RAY DIFFRACTIONr_mcbond_other2.5624.8953474
X-RAY DIFFRACTIONr_mcangle_it4.178.84340
X-RAY DIFFRACTIONr_mcangle_other4.178.8014341
X-RAY DIFFRACTIONr_scbond_it2.5385.2413639
X-RAY DIFFRACTIONr_scbond_other2.5375.2423640
X-RAY DIFFRACTIONr_scangle_it
X-RAY DIFFRACTIONr_scangle_other4.2499.5575342
X-RAY DIFFRACTIONr_long_range_B_refined7.64149.418413
X-RAY DIFFRACTIONr_long_range_B_other7.63749.438402
X-RAY DIFFRACTIONr_rigid_bond_restr
X-RAY DIFFRACTIONr_sphericity_free
X-RAY DIFFRACTIONr_sphericity_bonded
LS refinement shellResolution: 2.1→2.154 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.365 137 -
Rwork0.38 3161 -
obs--95.76 %

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