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- PDB-9hrr: Crystal structure of Arabidopsis thaliana Fatty Acid Thioesterase... -

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Basic information

Entry
Database: PDB / ID: 9hrr
TitleCrystal structure of Arabidopsis thaliana Fatty Acid Thioesterase A in an apo state
ComponentsOleoyl-acyl carrier protein thioesterase 1, chloroplastic
KeywordsHYDROLASE / Thioesterase / Plant / Fatty Acid Biosynthesis / Fatty Acid / Chain termination / Dimer / Acyl-ACP thioesterase / Acyl ACP thioesterase / 18:1 FA / FatA / ACP / Herbicide / Mode of Action
Function / homology
Function and homology information


oleoyl-[acyl-carrier-protein] hydrolase / fatty acyl-[ACP] hydrolase activity / acyl carrier activity / chloroplast / fatty acid biosynthetic process
Similarity search - Function
Acyl-ACP thioesterase / Acyl-[acyl-carrier-protein] hydrolase FATA/B / : / Acyl-ACP thioesterase N-terminal domain / Acyl-ACP thioesterase C-terminal domain / HotDog domain superfamily
Similarity search - Domain/homology
Oleoyl-acyl carrier protein thioesterase 1, chloroplastic
Similarity search - Component
Biological speciesArabidopsis thaliana (thale cress)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.64 Å
AuthorsKot, E. / Ni, X. / Koekemoer, L. / Mulholland, N.P. / Montgomery, M.G. / von Delft, F.
Funding support United Kingdom, 1items
OrganizationGrant numberCountry
Engineering and Physical Sciences Research Council United Kingdom
CitationJournal: Pest Manag Sci / Year: 2026
Title: Crystal structure of fatty acid thioesterase A bound by 129 fragments provides diverse development opportunities.
Authors: Kot, E. / Ferla, M.P. / Hollinshead, P.H. / Tomlinson, C.W.E. / Fearon, D. / Aschenbrenner, J.C. / Koekemoer, L. / Winokan, M. / Fairhead, M. / Ni, X. / Chalk, R. / England, K.S. / Varga, L. ...Authors: Kot, E. / Ferla, M.P. / Hollinshead, P.H. / Tomlinson, C.W.E. / Fearon, D. / Aschenbrenner, J.C. / Koekemoer, L. / Winokan, M. / Fairhead, M. / Ni, X. / Chalk, R. / England, K.S. / Varga, L.O. / Montgomery, M.G. / Mulholland, N.P. / von Delft, F.
History
DepositionDec 18, 2024Deposition site: PDBE / Processing site: PDBE
Revision 1.0Aug 13, 2025Provider: repository / Type: Initial release
Revision 1.1Mar 4, 2026Group: Database references / Category: citation / citation_author
Item: _citation.journal_abbrev / _citation.journal_id_CSD ..._citation.journal_abbrev / _citation.journal_id_CSD / _citation.journal_id_ISSN / _citation.journal_volume / _citation.page_first / _citation.page_last / _citation.pdbx_database_id_DOI / _citation.pdbx_database_id_PubMed / _citation.title / _citation.year

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: Oleoyl-acyl carrier protein thioesterase 1, chloroplastic
B: Oleoyl-acyl carrier protein thioesterase 1, chloroplastic
hetero molecules


Theoretical massNumber of molelcules
Total (without water)67,6156
Polymers67,2312
Non-polymers3844
Water3,117173
1


  • Idetical with deposited unit
  • defined by author&software
  • Evidence: mass spectrometry
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area4390 Å2
ΔGint-72 kcal/mol
Surface area24200 Å2
MethodPISA
Unit cell
Length a, b, c (Å)98.818, 98.815, 128.771
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number23
Space group name H-MI222

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Components

#1: Protein Oleoyl-acyl carrier protein thioesterase 1, chloroplastic / 18:0-acyl-carrier protein thioesterase / 18:0-ACP thioesterase / Acyl-[acyl-carrier-protein] hydrolase


Mass: 33615.598 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Details: The N-terminal chloroplast transit peptide (residues 1-74) has been removed. A C-terminal His6 tag was added.
Source: (gene. exp.) Arabidopsis thaliana (thale cress) / Gene: FATA, FATA1, At3g25110, MJL12.5 / Production host: Escherichia coli (E. coli)
References: UniProt: Q42561, oleoyl-[acyl-carrier-protein] hydrolase
#2: Chemical
ChemComp-SO4 / SULFATE ION


Mass: 96.063 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: SO4
#3: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 173 / Source method: isolated from a natural source / Formula: H2O
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: 2.34 Å3/Da / Density % sol: 47.39 %
Crystal growTemperature: 293 K / Method: vapor diffusion, sitting drop / pH: 6.85 / Details: 0.1M MES pH 6.85, 1.6M Ammonium sulfate

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: Diamond / Beamline: I04-1 / Wavelength: 0.9212 Å
DetectorType: DECTRIS EIGER2 XE 9M / Detector: PIXEL / Date: Mar 8, 2023
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9212 Å / Relative weight: 1
ReflectionResolution: 1.64→78.4 Å / Num. obs: 76807 / % possible obs: 99.5 % / Redundancy: 13.6 % / CC1/2: 0.999 / Rmerge(I) obs: 0.119 / Rpim(I) all: 0.033 / Rrim(I) all: 0.124 / Net I/σ(I): 10.3 / Num. measured all: 1043747
Reflection shellResolution: 1.64→1.67 Å / % possible obs: 98.8 % / Redundancy: 11.9 % / Rmerge(I) obs: 3.327 / Num. measured all: 44908 / Num. unique obs: 3769 / CC1/2: 0.395 / Rpim(I) all: 0.993 / Rrim(I) all: 3.476 / Net I/σ(I) obs: 0.3

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Processing

Software
NameVersionClassification
REFMAC5.8.0425refinement
DIALSdata scaling
xia2data reduction
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT / Resolution: 1.64→78.4 Å / Cor.coef. Fo:Fc: 0.96 / Cor.coef. Fo:Fc free: 0.94 / SU B: 3.833 / SU ML: 0.114 / Cross valid method: THROUGHOUT / ESU R: 0.102 / ESU R Free: 0.108 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN USED IF PRESENT IN THE INPUT
RfactorNum. reflection% reflectionSelection details
Rfree0.26069 4025 5.2 %RANDOM
Rwork0.21394 ---
obs0.21628 72781 99.41 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK
Displacement parametersBiso mean: 36.747 Å2
Baniso -1Baniso -2Baniso -3
1--0.42 Å20 Å2-0 Å2
2---0.64 Å20 Å2
3---1.06 Å2
Refinement stepCycle: 1 / Resolution: 1.64→78.4 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms4243 0 20 173 4436
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0070.0124384
X-RAY DIFFRACTIONr_bond_other_d0.0020.0164155
X-RAY DIFFRACTIONr_angle_refined_deg1.61.8385942
X-RAY DIFFRACTIONr_angle_other_deg0.5451.7939548
X-RAY DIFFRACTIONr_dihedral_angle_1_deg6.1755532
X-RAY DIFFRACTIONr_dihedral_angle_2_deg7.826541
X-RAY DIFFRACTIONr_dihedral_angle_3_deg13.1710796
X-RAY DIFFRACTIONr_dihedral_angle_4_deg
X-RAY DIFFRACTIONr_chiral_restr0.0770.2671
X-RAY DIFFRACTIONr_gen_planes_refined0.0060.025220
X-RAY DIFFRACTIONr_gen_planes_other0.0010.021036
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_it2.8953.2582110
X-RAY DIFFRACTIONr_mcbond_other2.8943.2572110
X-RAY DIFFRACTIONr_mcangle_it4.0185.8232627
X-RAY DIFFRACTIONr_mcangle_other4.0175.8242628
X-RAY DIFFRACTIONr_scbond_it4.3763.9322274
X-RAY DIFFRACTIONr_scbond_other4.3473.9222259
X-RAY DIFFRACTIONr_scangle_it
X-RAY DIFFRACTIONr_scangle_other6.8986.8993285
X-RAY DIFFRACTIONr_long_range_B_refined8.43532.114557
X-RAY DIFFRACTIONr_long_range_B_other8.4432.114541
X-RAY DIFFRACTIONr_rigid_bond_restr
X-RAY DIFFRACTIONr_sphericity_free
X-RAY DIFFRACTIONr_sphericity_bonded
LS refinement shellResolution: 1.64→1.682 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.381 262 -
Rwork0.378 5206 -
obs--97.63 %

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