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- PDB-3t2e: Fructose-1,6-bisphosphate aldolase/phosphatase from Thermoproteus... -

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Basic information

Entry
Database: PDB / ID: 3t2e
TitleFructose-1,6-bisphosphate aldolase/phosphatase from Thermoproteus neutrophilus, F6P-bound form
ComponentsFructose-1,6-bisphosphate aldolase/phosphatase
KeywordsLYASE / HYDROLASE / (beta/alpha)8 TIM barrel / FBP / F6P / DHAP / GAP / phosphorylation
Function / homology
Function and homology information


fructose-bisphosphate aldolase / fructose-bisphosphate aldolase activity / fructose-bisphosphatase / fructose 1,6-bisphosphate 1-phosphatase activity / gluconeogenesis / magnesium ion binding
Similarity search - Function
Single alpha-helices involved in coiled-coils or other helix-helix interfaces - #1180 / Fructose-1,6-bisphosphatase, class V / Fructose-1,6-bisphosphatase, class V superfamily / Fructose-1,6-bisphosphatase / Single alpha-helices involved in coiled-coils or other helix-helix interfaces / Helix non-globular / Special
Similarity search - Domain/homology
FRUCTOSE -6-PHOSPHATE / Fructose-1,6-bisphosphate aldolase/phosphatase
Similarity search - Component
Biological speciesThermoproteus neutrophilus (archaea)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.66 Å
AuthorsDu, J. / Say, R. / Lue, W. / Fuchs, G. / Einsle, O.
CitationJournal: Nature / Year: 2011
Title: Active-site remodelling in the bifunctional fructose-1,6-bisphosphate aldolase/phosphatase.
Authors: Du, J. / Say, R.F. / Lu, W. / Fuchs, G. / Einsle, O.
History
DepositionJul 22, 2011Deposition site: RCSB / Processing site: RCSB
Revision 1.0Oct 26, 2011Provider: repository / Type: Initial release
Revision 1.1Nov 9, 2011Group: Database references
Revision 1.2Sep 13, 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_conn_angle / struct_conn / 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 / _pdbx_struct_conn_angle.ptnr1_auth_comp_id / _pdbx_struct_conn_angle.ptnr1_auth_seq_id / _pdbx_struct_conn_angle.ptnr1_label_asym_id / _pdbx_struct_conn_angle.ptnr1_label_atom_id / _pdbx_struct_conn_angle.ptnr1_label_comp_id / _pdbx_struct_conn_angle.ptnr1_label_seq_id / _pdbx_struct_conn_angle.ptnr3_auth_comp_id / _pdbx_struct_conn_angle.ptnr3_auth_seq_id / _pdbx_struct_conn_angle.ptnr3_label_asym_id / _pdbx_struct_conn_angle.ptnr3_label_atom_id / _pdbx_struct_conn_angle.ptnr3_label_comp_id / _pdbx_struct_conn_angle.ptnr3_label_seq_id / _pdbx_struct_conn_angle.value / _struct_conn.pdbx_dist_value / _struct_conn.ptnr1_auth_comp_id / _struct_conn.ptnr1_auth_seq_id / _struct_conn.ptnr1_label_asym_id / _struct_conn.ptnr1_label_atom_id / _struct_conn.ptnr1_label_comp_id / _struct_conn.ptnr1_label_seq_id / _struct_conn.ptnr2_auth_comp_id / _struct_conn.ptnr2_auth_seq_id / _struct_conn.ptnr2_label_asym_id / _struct_conn.ptnr2_label_atom_id / _struct_conn.ptnr2_label_comp_id / _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: Fructose-1,6-bisphosphate aldolase/phosphatase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)45,7704
Polymers45,4611
Non-polymers3093
Water4,972276
1
A: Fructose-1,6-bisphosphate aldolase/phosphatase
hetero molecules
x 8


Theoretical massNumber of molelcules
Total (without water)366,15832
Polymers363,6888
Non-polymers2,47024
Water1448
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation2_465-x-1,-y+1,z1
crystal symmetry operation3_565-y,x+1,z1
crystal symmetry operation4_455y-1,-x,z1
crystal symmetry operation5_455-x-1,y,-z1
crystal symmetry operation6_565x,-y+1,-z1
crystal symmetry operation7_465y-1,x+1,-z1
crystal symmetry operation8_555-y,-x,-z1
Buried area65060 Å2
ΔGint-546 kcal/mol
Surface area81940 Å2
MethodPISA
Unit cell
Length a, b, c (Å)112.308, 112.308, 151.221
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number97
Space group name H-MI422
Components on special symmetry positions
IDModelComponents
11A-454-

HOH

21A-560-

HOH

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Components

#1: Protein Fructose-1,6-bisphosphate aldolase/phosphatase


Mass: 45461.031 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Thermoproteus neutrophilus (archaea) / Strain: DSM 2338 / JCM 9278 / V24Sta / Gene: Tneu_0133 / Plasmid: pET23b / Production host: Escherichia coli (E. coli)
References: UniProt: B1YAL1, fructose-bisphosphate aldolase, fructose-bisphosphatase
#2: Chemical ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Mg
#3: Chemical ChemComp-F6R / FRUCTOSE -6-PHOSPHATE


Mass: 260.136 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C6H13O9P
#4: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 276 / 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: 2.62 Å3/Da / Density % sol: 53.09 %
Crystal growTemperature: 294 K / Method: vapor diffusion, hanging drop / pH: 7.5
Details: 8% PEG3350, 0.1 M HEPES/NaOH, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 294K

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Data collection

DiffractionMean temperature: 90 K
Diffraction sourceSource: SYNCHROTRON / Site: SLS / Beamline: X06SA / Wavelength: 1 / Wavelength: 1 Å
DetectorType: PSI PILATUS 6M / Detector: PIXEL / Date: Aug 1, 2010
RadiationMonochromator: Fixed-exit LN2 cooled Double Crystal / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelength
IDWavelength (Å)Relative weight
111
211
ReflectionResolution: 1.66→39.707 Å / Num. all: 57129 / Num. obs: 57043 / % possible obs: 99.8 % / Observed criterion σ(F): 2 / Observed criterion σ(I): 2 / Redundancy: 8 % / Rmerge(I) obs: 0.094 / Rsym value: 0.094 / Net I/σ(I): 15.3
Reflection shellResolution: 1.66→1.7 Å / Redundancy: 7.3 % / Rmerge(I) obs: 0.371 / Mean I/σ(I) obs: 5.2 / Rsym value: 0.371 / % possible all: 99.9

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Processing

Software
NameVersionClassification
MAR345dtbdata collection
MOLREPphasing
REFMAC5.5.0109refinement
XDSdata reduction
SCALAdata scaling
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB ENTRY 3T2B

3t2b


Resolution: 1.66→39.707 Å / Cor.coef. Fo:Fc: 0.965 / Cor.coef. Fo:Fc free: 0.955 / SU B: 1.235 / SU ML: 0.043 / Cross valid method: THROUGHOUT / σ(F): 2 / ESU R: 0.073 / ESU R Free: 0.075 / Stereochemistry target values: MAXIMUM LIKELIHOOD
Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS U VALUES : REFINED INDIVIDUALLY
RfactorNum. reflection% reflectionSelection details
Rfree0.17798 2892 5.1 %RANDOM
Rwork0.14996 ---
obs0.15138 54151 99.84 %-
all-54151 --
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: MASK
Displacement parametersBiso mean: 16.546 Å2
Baniso -1Baniso -2Baniso -3
1-0.13 Å2-0 Å2-0 Å2
2--0.13 Å20 Å2
3----0.26 Å2
Refinement stepCycle: LAST / Resolution: 1.66→39.707 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms3025 0 18 276 3319
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0320.0223153
X-RAY DIFFRACTIONr_angle_refined_deg2.4351.984277
X-RAY DIFFRACTIONr_dihedral_angle_1_deg6.5765392
X-RAY DIFFRACTIONr_dihedral_angle_2_deg36.02923.169142
X-RAY DIFFRACTIONr_dihedral_angle_3_deg14.90715528
X-RAY DIFFRACTIONr_dihedral_angle_4_deg15.7481523
X-RAY DIFFRACTIONr_chiral_restr0.1990.2458
X-RAY DIFFRACTIONr_gen_planes_refined0.0140.0212426
X-RAY DIFFRACTIONr_mcbond_it1.5561.51934
X-RAY DIFFRACTIONr_mcangle_it2.56923116
X-RAY DIFFRACTIONr_scbond_it3.79331219
X-RAY DIFFRACTIONr_scangle_it6.1194.51156
LS refinement shellResolution: 1.66→1.703 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.231 193 -
Rwork0.21 3967 -
obs--99.83 %

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