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- PDB-4tu1: Structure of Toxoplasma gondii fructose 1,6 bisphosphate aldolase -

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Basic information

Entry
Database: PDB / ID: 4tu1
TitleStructure of Toxoplasma gondii fructose 1,6 bisphosphate aldolase
ComponentsFructose-1,6-bisphosphate aldolase
KeywordsLYASE / aldolase / F16BP / invasion / toxoplasma / glideosome / Structural Genomics / PSI-2 / Protein Structure Initiative / Seattle Structural Genomics Center for Infectious Disease / SSGCID
Function / homology
Function and homology information


apical cytoplasm / biological process involved in symbiotic interaction / adhesion of symbiont to host cell / symbiont entry into host / fructose-bisphosphate aldolase / fructose-bisphosphate aldolase activity / fructose 1,6-bisphosphate metabolic process / positive regulation of ATP biosynthetic process / glycolytic process / actin filament binding ...apical cytoplasm / biological process involved in symbiotic interaction / adhesion of symbiont to host cell / symbiont entry into host / fructose-bisphosphate aldolase / fructose-bisphosphate aldolase activity / fructose 1,6-bisphosphate metabolic process / positive regulation of ATP biosynthetic process / glycolytic process / actin filament binding / positive regulation of cell population proliferation / extracellular space / membrane
Similarity search - Function
Fructose-bisphosphate aldolase class-I active site / Fructose-bisphosphate aldolase class-I active site. / Fructose-bisphosphate aldolase, class-I / Fructose-bisphosphate aldolase class-I / Aldolase class I / Aldolase-type TIM barrel / TIM Barrel / Alpha-Beta Barrel / Alpha Beta
Similarity search - Domain/homology
Fructose-bisphosphate aldolase
Similarity search - Component
Biological speciesToxoplasma gondii (eukaryote)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2 Å
AuthorsBoucher, L.E. / Bosch, J. / Seattle Structural Genomics Center for Infectious Disease (SSGCID)
CitationJournal: Acta Crystallogr.,Sect.F / Year: 2014
Title: Structure of Toxoplasma gondii fructose-1,6-bisphosphate aldolase.
Authors: Boucher, L.E. / Bosch, J.
History
DepositionJun 23, 2014Deposition site: RCSB / Processing site: RCSB
Revision 1.0Sep 3, 2014Provider: repository / Type: Initial release
Revision 1.1Sep 24, 2014Group: Database references
Revision 1.2Nov 22, 2017Group: Derived calculations / Other ...Derived calculations / Other / Refinement description / Source and taxonomy
Category: entity_src_gen / pdbx_database_status ...entity_src_gen / pdbx_database_status / pdbx_struct_assembly / pdbx_struct_assembly_gen / pdbx_struct_assembly_prop / pdbx_struct_oper_list / software
Item: _entity_src_gen.pdbx_alt_source_flag / _pdbx_database_status.pdb_format_compatible ..._entity_src_gen.pdbx_alt_source_flag / _pdbx_database_status.pdb_format_compatible / _pdbx_struct_assembly.oligomeric_details / _pdbx_struct_assembly_gen.asym_id_list / _pdbx_struct_assembly_prop.type / _pdbx_struct_assembly_prop.value / _pdbx_struct_oper_list.symmetry_operation / _software.classification
Revision 1.3Sep 27, 2023Group: Data collection / Database references / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model / refine_hist
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession

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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
B: Fructose-1,6-bisphosphate aldolase
C: Fructose-1,6-bisphosphate aldolase
D: Fructose-1,6-bisphosphate aldolase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)154,3095
Polymers154,2164
Non-polymers921
Water17,114950
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area9170 Å2
ΔGint-44 kcal/mol
Surface area51310 Å2
MethodPISA
Unit cell
Length a, b, c (Å)92.258, 134.458, 162.430
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number18
Space group name H-MP22121

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Components

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


Mass: 38554.117 Da / Num. of mol.: 4 / Fragment: UNP residues 78-410
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Toxoplasma gondii (eukaryote) / Gene: TGVEG_236040 / Plasmid: pET14b / Production host: Escherichia coli (E. coli) / Strain (production host): BL21 DE3 / References: UniProt: B9PW35, fructose-bisphosphate aldolase
#2: Chemical ChemComp-GOL / GLYCEROL / GLYCERIN / PROPANE-1,2,3-TRIOL / Glycerol


Mass: 92.094 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C3H8O3
#3: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 950 / Source method: isolated from a natural source / Formula: H2O

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION

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Sample preparation

CrystalDensity Matthews: 3.27 Å3/Da / Density % sol: 62.34 %
Crystal growTemperature: 277 K / Method: vapor diffusion, sitting drop / pH: 7.9
Details: 0.1 M MOP/HEPES pH 7.9, 0.02 M sodium formate, 0.02 M ammonium acetate, 0.02 M trisodium citrate, 0.02 M sodium potassium L-tartrate, 0.02 M sodium oxamate, 0.02 M ammonium acetate, 12.5% ...Details: 0.1 M MOP/HEPES pH 7.9, 0.02 M sodium formate, 0.02 M ammonium acetate, 0.02 M trisodium citrate, 0.02 M sodium potassium L-tartrate, 0.02 M sodium oxamate, 0.02 M ammonium acetate, 12.5% glycerol, 25% PEG-4000; seeded

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: SSRL / Beamline: BL7-1 / Wavelength: 1.127092 Å
DetectorType: ADSC QUANTUM 315r / Detector: CCD / Date: May 9, 2014
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.127092 Å / Relative weight: 1
ReflectionResolution: 1.749→46.7 Å / Num. all: 184014 / Num. obs: 184014 / % possible obs: 90.49 % / Redundancy: 3.6 % / Rmerge(I) obs: 0.0777 / Net I/σ(I): 11.44
Reflection shellResolution: 1.749→1.812 Å / Redundancy: 3.2 % / Rmerge(I) obs: 1.858 / Mean I/σ(I) obs: 0.61 / % possible all: 58.27

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Processing

Software
NameVersionClassification
PHENIX(phenix.refine: 1.9_1692)refinement
Cootmodel building
Blu-Icedata collection
PHASERphasing
XDSdata scaling
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 2PC4
Resolution: 2→46.696 Å / SU ML: 0.23 / Cross valid method: FREE R-VALUE / σ(F): 1.36 / Phase error: 29.95 / Stereochemistry target values: ML
RfactorNum. reflection% reflectionSelection details
Rfree0.2442 6505 4.93 %Random selection
Rwork0.194 ---
obs0.1964 132055 96.63 %-
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Refinement stepCycle: LAST / Resolution: 2→46.696 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms10277 0 6 950 11233
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00710510
X-RAY DIFFRACTIONf_angle_d1.01514213
X-RAY DIFFRACTIONf_dihedral_angle_d12.6813977
X-RAY DIFFRACTIONf_chiral_restr0.0391601
X-RAY DIFFRACTIONf_plane_restr0.0051861
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2-2.02270.37232450.31854140X-RAY DIFFRACTION98
2.0227-2.04650.30842130.29134207X-RAY DIFFRACTION98
2.0465-2.07150.44362090.38393967X-RAY DIFFRACTION93
2.0715-2.09770.31421930.28734049X-RAY DIFFRACTION94
2.0977-2.12530.35142170.2514146X-RAY DIFFRACTION97
2.1253-2.15440.30862290.24534198X-RAY DIFFRACTION98
2.1544-2.18520.28312250.2324138X-RAY DIFFRACTION98
2.1852-2.21780.28492130.23134206X-RAY DIFFRACTION98
2.2178-2.25250.42491650.35033659X-RAY DIFFRACTION84
2.2525-2.28940.32831940.25453827X-RAY DIFFRACTION89
2.2894-2.32890.30461890.22334260X-RAY DIFFRACTION98
2.3289-2.37120.30161950.21514232X-RAY DIFFRACTION98
2.3712-2.41680.2552230.21144206X-RAY DIFFRACTION98
2.4168-2.46620.24992450.20434182X-RAY DIFFRACTION98
2.4662-2.51980.26692270.20484218X-RAY DIFFRACTION98
2.5198-2.57840.26532240.20264232X-RAY DIFFRACTION98
2.5784-2.64290.26782330.21044215X-RAY DIFFRACTION98
2.6429-2.71430.26952170.224139X-RAY DIFFRACTION96
2.7143-2.79420.25712190.20924229X-RAY DIFFRACTION98
2.7942-2.88440.28492060.2094265X-RAY DIFFRACTION98
2.8844-2.98740.25482030.20534264X-RAY DIFFRACTION98
2.9874-3.1070.26852310.20054224X-RAY DIFFRACTION98
3.107-3.24840.23972220.19284237X-RAY DIFFRACTION98
3.2484-3.41960.23622230.18394262X-RAY DIFFRACTION98
3.4196-3.63380.23941960.18464223X-RAY DIFFRACTION97
3.6338-3.91420.21972420.16314127X-RAY DIFFRACTION95
3.9142-4.30790.19861930.14634327X-RAY DIFFRACTION97
4.3079-4.93060.15032270.13434283X-RAY DIFFRACTION97
4.9306-6.20980.1982500.15644402X-RAY DIFFRACTION99
6.2098-46.70860.18562370.14624486X-RAY DIFFRACTION97
Refinement TLS params.

Method: refined / Refine-ID: X-RAY DIFFRACTION

IDL112)L122)L132)L222)L232)L332)S11 (Å °)S12 (Å °)S13 (Å °)S21 (Å °)S22 (Å °)S23 (Å °)S31 (Å °)S32 (Å °)S33 (Å °)T112)T122)T132)T222)T232)T332)Origin x (Å)Origin y (Å)Origin z (Å)
12.9716-2.6268-2.01876.89314.29767.26490.12030.25920.4418-0.3303-0.23710.0537-0.9167-0.30470.04420.2693-0.0769-0.02840.28150.08590.319736.586654.924720.1132
21.3310.1155-0.53760.32250.24241.4624-0.04410.19270.0061-0.0973-0.0073-0.0353-0.05550.25350.07370.26260.0165-0.02680.3580.02970.235248.660641.344419.6302
32.00890.1960.15610.920.20631.6314-0.0580.3463-0.1781-0.12240.00870.01670.0735-0.0180.03140.19810.01660.00730.2137-0.02050.17828.514138.172822.3706
45.0393-0.304-2.06921.31080.15373.1553-0.11260.6340.0586-0.10880.0223-0.0555-0.0759-0.01280.10540.2728-0.0012-0.02530.5197-0.01710.199141.188838.27323.4757
56.5275-1.9312.07736.3683-3.06864.12750.30640.9992-0.0944-0.5758-0.30210.51840.39890.04650.03190.3156-0.0503-0.01390.6484-0.09030.34182.056341.68818.2696
65.1325-1.02221.96095.5409-0.47784.71150.156-0.03451.45070.375-0.23650.4725-0.69810.02450.10090.37260.01610.01270.50530.0350.779-17.054655.981923.5336
72.55510.23972.53240.6313-0.19342.7049-0.05290.16040.1255-0.03480.06560.0059-0.1036-0.5674-0.03320.21570.0350.01330.3362-0.0360.2964-6.658445.762329.9657
81.44280.2837-0.42721.47110.2371.7520.00720.13420.23140.0520.00280.1064-0.2415-0.13220.0210.2440.0669-0.04130.184-0.01020.264910.114252.362132.3511
93.0805-1.09760.3283.313-1.15842.5952-0.15350.30690.5979-0.27450.06190.5112-0.6192-0.27650.0960.46060.1111-0.07230.3290.06810.380712.391160.90519.9231
106.03180.28910.16410.59910.24662.65720.02791.21881.9398-0.41750.0960.4306-0.44020.0478-0.13930.58260.0445-0.01810.79230.33291.0654-10.572863.634516.3768
117.71884.52040.82466.68080.17583.99350.003-0.7309-0.07650.1754-0.1188-0.3549-0.37810.10490.11690.26230.05280.00190.4696-0.04130.23416.169439.160365.0096
122.21920.4855-1.58250.2485-0.64253.3639-0.09-0.1982-0.20050.05160.07340.0420.4079-0.5578-0.0010.2761-0.0611-0.0110.42830.01980.3313-7.965529.122958.4983
132.1112-0.9688-0.51831.28670.62661.868-0.0598-0.0548-0.31620.0453-0.05290.06470.1789-0.00430.11970.2125-0.01340.00660.1570.01070.253411.580130.51648.7603
141.8479-0.2550.04292.63340.06592.3109-0.1864-0.4221-0.67330.13180.12870.2760.477-0.00660.05430.28250.00140.06920.27910.08230.44115.800121.518558.5739
154.13823.5569-1.00323.8042-1.15624.16140.0197-0.1296-0.69140.4744-0.0170.09830.62840.44640.04730.5126-0.03130.09490.4650.03750.49372.054519.596265.17
165.53571.767-2.27975.0975-0.30774.874-0.0424-1.399-1.57090.616-0.2608-0.50860.81970.41310.21970.6266-0.06130.04440.79640.32750.6685-4.254415.343673.0311
174.24783.91076.034.0974.64732.0836-0.2246-0.9582-0.7285-0.0248-0.34320.25680.4443-0.32260.20860.3737-0.01240.01670.57220.10480.4937.993322.418954.8375
184.00082.8515-2.47496.7277-1.6134.2403-0.02650.85731.36260.1154-0.3116-0.5967-1.21160.45930.36970.6972-0.2429-0.18751.1190.47630.887954.335447.722164.1589
192.17262.5125-1.16325.011-0.92743.3947-0.28660.33420.2677-0.8099-0.0994-1.1413-0.0091.05480.53280.4356-0.02830.05981.00720.25060.653460.060640.743468.6139
206.2362-2.03622.51951.3155-0.0831.83110.09920.47-0.13640.0674-0.2834-0.3753-0.42060.84040.21630.2853-0.0806-0.02020.68680.13260.38659.284735.245758.9717
211.9006-0.75341.49692.0361-1.16573.40490.0077-0.1634-0.08960.0421-0.076-0.09430.01150.44950.12920.163-0.02850.0190.33960.03680.18847.442639.428449.7233
221.625-0.1432-0.36271.5704-0.16091.4686-0.0265-0.25820.11720.093-0.01550.0761-0.16740.22340.0230.2167-0.0244-0.03090.2516-0.02590.173333.165845.222653.4607
232.745-1.12721.72743.77030.79873.9861-0.1805-1.25550.11250.52560.2855-0.3012-0.08970.501-0.05680.3354-0.0289-0.00860.6898-0.05650.285531.288644.37468.196
240.4335-0.261-0.84551.4216-1.11053.6745-0.44210.71071.3890.3114-0.1664-0.5369-0.46190.78090.49520.4415-0.0533-0.15840.77530.36520.740255.073845.063275.0656
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1chain 'A' and (resid 16 through 52 )
2X-RAY DIFFRACTION2chain 'A' and (resid 53 through 177 )
3X-RAY DIFFRACTION3chain 'A' and (resid 178 through 289 )
4X-RAY DIFFRACTION4chain 'A' and (resid 290 through 355 )
5X-RAY DIFFRACTION5chain 'B' and (resid 17 through 52 )
6X-RAY DIFFRACTION6chain 'B' and (resid 53 through 100 )
7X-RAY DIFFRACTION7chain 'B' and (resid 101 through 156 )
8X-RAY DIFFRACTION8chain 'B' and (resid 157 through 262 )
9X-RAY DIFFRACTION9chain 'B' and (resid 263 through 312 )
10X-RAY DIFFRACTION10chain 'B' and (resid 313 through 355 )
11X-RAY DIFFRACTION11chain 'C' and (resid 17 through 52 )
12X-RAY DIFFRACTION12chain 'C' and (resid 53 through 156 )
13X-RAY DIFFRACTION13chain 'C' and (resid 157 through 236 )
14X-RAY DIFFRACTION14chain 'C' and (resid 237 through 306 )
15X-RAY DIFFRACTION15chain 'C' and (resid 307 through 333 )
16X-RAY DIFFRACTION16chain 'C' and (resid 334 through 355 )
17X-RAY DIFFRACTION17chain 'D' and (resid 18 through 39 )
18X-RAY DIFFRACTION18chain 'D' and (resid 40 through 63 )
19X-RAY DIFFRACTION19chain 'D' and (resid 64 through 88 )
20X-RAY DIFFRACTION20chain 'D' and (resid 89 through 108 )
21X-RAY DIFFRACTION21chain 'D' and (resid 109 through 156 )
22X-RAY DIFFRACTION22chain 'D' and (resid 157 through 262 )
23X-RAY DIFFRACTION23chain 'D' and (resid 263 through 318 )
24X-RAY DIFFRACTION24chain 'D' and (resid 319 through 355 )

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