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- PDB-6o4n: Crystal Structure of Enolase from Chlamydia trachomatis -

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Basic information

Entry
Database: PDB / ID: 6o4n
TitleCrystal Structure of Enolase from Chlamydia trachomatis
ComponentsEnolase
KeywordsHYDROLASE / SSGCID / enolase / 2-phospho-D-glycerate hydro-lyase / 2-phosphoglycerate dehydratase / strain D/UW-3/Cx / Structural Genomics / Seattle Structural Genomics Center for Infectious Disease
Function / homology
Function and homology information


phosphopyruvate hydratase / phosphopyruvate hydratase complex / phosphopyruvate hydratase activity / glycolytic process / cell surface / magnesium ion binding / extracellular region
Similarity search - Function
Enolase / Enolase, conserved site / Enolase, C-terminal TIM barrel domain / Enolase, N-terminal / Enolase, C-terminal TIM barrel domain / Enolase, N-terminal domain / Enolase signature. / Enolase, C-terminal TIM barrel domain / Enolase, N-terminal domain / Enolase-like C-terminal domain ...Enolase / Enolase, conserved site / Enolase, C-terminal TIM barrel domain / Enolase, N-terminal / Enolase, C-terminal TIM barrel domain / Enolase, N-terminal domain / Enolase signature. / Enolase, C-terminal TIM barrel domain / Enolase, N-terminal domain / Enolase-like C-terminal domain / Enolase-like, N-terminal domain / Enolase-like, N-terminal / Enolase-like, C-terminal domain superfamily / Enolase-like; domain 1 / TIM Barrel / Alpha-Beta Barrel / 2-Layer Sandwich / Alpha Beta
Similarity search - Domain/homology
PHOSPHATE ION / Enolase
Similarity search - Component
Biological speciesChlamydia trachomatis serovar L2b
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / molecular replacement / Resolution: 1.8 Å
AuthorsSeattle Structural Genomics Center for Infectious Disease (SSGCID)
CitationJournal: to be published
Title: Crystal Structure of Enolase from Chlamydia trachomatis
Authors: Dranow, D.M. / Mayclin, S.J. / Lorimer, D.D. / Horanyi, P.S. / Edwards, T.E.
History
DepositionFeb 28, 2019Deposition site: RCSB / Processing site: RCSB
Revision 1.0Mar 13, 2019Provider: repository / Type: Initial release
Revision 1.1Oct 11, 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
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_seq_id / _pdbx_struct_conn_angle.ptnr3_auth_seq_id / _pdbx_struct_conn_angle.value / _struct_conn.pdbx_dist_value / _struct_conn.ptnr1_auth_asym_id / _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_asym_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

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Enolase
B: Enolase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)94,32322
Polymers93,0072
Non-polymers1,31620
Water15,997888
1


  • Idetical with deposited unit
  • defined by author
  • Evidence: gel filtration
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area7240 Å2
ΔGint-114 kcal/mol
Surface area27470 Å2
Unit cell
Length a, b, c (Å)164.280, 164.280, 89.790
Angle α, β, γ (deg.)90.000, 90.000, 90.000
Int Tables number79
Space group name H-MI4

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Components

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Protein , 1 types, 2 molecules AB

#1: Protein Enolase / 2-phospho-D-glycerate hydro-lyase / 2-phosphoglycerate dehydratase


Mass: 46503.457 Da / Num. of mol.: 2 / Fragment: ChtrB.00084.a.B1 / Mutation: M78V,T178K
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Chlamydia trachomatis serovar L2b (strain UCH-1/proctitis) (bacteria)
Strain: UCH-1/proctitis / Gene: eno, CTLon_0844 / Plasmid: CChtrB.00084.a.B1 / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: B0BA40, phosphopyruvate hydratase

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Non-polymers , 6 types, 908 molecules

#2: Chemical
ChemComp-MRD / (4R)-2-METHYLPENTANE-2,4-DIOL


Mass: 118.174 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C6H14O2 / Comment: precipitant*YM
#3: Chemical
ChemComp-EDO / 1,2-ETHANEDIOL / ETHYLENE GLYCOL


Mass: 62.068 Da / Num. of mol.: 8 / Source method: obtained synthetically / Formula: C2H6O2
#4: Chemical ChemComp-PO4 / PHOSPHATE ION


Mass: 94.971 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: PO4
#5: Chemical
ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 5 / Source method: obtained synthetically / Formula: Mg
#6: Chemical ChemComp-CL / CHLORIDE ION


Mass: 35.453 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: Cl
#7: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 888 / 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: 2

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Sample preparation

CrystalDensity Matthews: 3.26 Å3/Da / Density % sol: 62.23 %
Crystal growTemperature: 287 K / Method: vapor diffusion, sitting drop / pH: 8.5
Details: ChtrB.00084.a.B1.PW38531 at 13.38 mg/ml was incubated with 2 mM 2-Phosphoglyceric acid, then was mixed 1:1 with Morpheus(e12): 12.5% (w/v) PEG 1000, 12.5% (w/v) PEG 3350, 12.5% (v/v) MPD, 0. ...Details: ChtrB.00084.a.B1.PW38531 at 13.38 mg/ml was incubated with 2 mM 2-Phosphoglyceric acid, then was mixed 1:1 with Morpheus(e12): 12.5% (w/v) PEG 1000, 12.5% (w/v) PEG 3350, 12.5% (v/v) MPD, 0.1 M bicine/Trizma base, pH 8.5, and 0.03 M each diethyleneglycol, triethyleneglycol, tetraethyleneglycol, pentaethyleneglycol. Tray: 305547e12, puck: vvm7-8.

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 21-ID-F / Wavelength: 0.97872 Å
DetectorType: RAYONIX MX-300 / Detector: CCD / Date: Feb 7, 2019 / Details: Beryllium Lenses
RadiationMonochromator: Diamond [111] / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.97872 Å / Relative weight: 1
ReflectionResolution: 1.8→41.876 Å / Num. obs: 110319 / % possible obs: 99.9 % / Redundancy: 5.082 % / Biso Wilson estimate: 32.418 Å2 / CC1/2: 0.997 / Rmerge(I) obs: 0.072 / Rrim(I) all: 0.08 / Χ2: 0.984 / Net I/σ(I): 13.5 / Num. measured all: 560618 / Scaling rejects: 10
Reflection shell

Diffraction-ID: 1

Resolution (Å)Redundancy (%)Rmerge(I) obsMean I/σ(I) obsNum. measured obsNum. possibleNum. unique obsCC1/2Rrim(I) all% possible all
1.8-1.855.060.562.840882808380790.8210.624100
1.85-1.95.0730.4143.7440217793279270.8980.46299.9
1.9-1.955.060.3414.6139221776077510.9290.38199.9
1.95-2.015.0840.256.0237988747474720.9590.279100
2.01-2.085.0830.2017.4937042729172880.970.224100
2.08-2.155.0980.169.0935703700470040.980.178100
2.15-2.235.1050.1310.9234662679367900.9870.145100
2.23-2.325.0250.11612.1832662650765000.9880.1399.9
2.32-2.435.1070.09813.9632112628962880.9920.109100
2.43-2.555.1110.08615.6730618599459910.9930.09699.9
2.55-2.685.1130.07717.3729122569756960.9940.085100
2.68-2.855.1160.06919.1527594539553940.9950.076100
2.85-3.045.1130.06321.0725972508150800.9950.07100
3.04-3.295.110.05923.0224251474947460.9950.06599.9
3.29-3.65.1070.05424.9522155434143380.9950.0699.9
3.6-4.025.0750.05326.1920091395939590.9960.059100
4.02-4.655.080.05227.2617699349134840.9960.05899.8
4.65-5.695.0570.05327.0514934295929530.9960.05999.8
5.69-8.055.0270.05426.9711531230222940.9950.0699.7
8.05-41.8764.7950.05427.66162130712850.9950.06198.3

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Phasing

PhasingMethod: molecular replacement

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Processing

Software
NameVersionClassification
XDSdata reduction
XSCALEdata scaling
PHENIXrefinement
PDB_EXTRACT3.24data extraction
MoRDaphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 4MKS
Resolution: 1.8→41.876 Å / SU ML: 0.16 / Cross valid method: FREE R-VALUE / σ(F): 0 / Phase error: 15.14
RfactorNum. reflection% reflectionSelection details
Rfree0.163 6502 6.1 %RANDOM, 0
Rwork0.1374 ---
obs0.1389 106510 96.48 %-
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å
Displacement parametersBiso max: 117.58 Å2 / Biso mean: 30.7026 Å2 / Biso min: 12.12 Å2
Refinement stepCycle: final / Resolution: 1.8→41.876 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms6313 0 88 893 7294
Biso mean--52.85 41.98 -
Num. residues----844
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Rfactor Rfree error: 0 / Total num. of bins used: 30

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkNum. reflection all% reflection obs (%)
1.8-1.82050.2532030.223009321288
1.8205-1.84190.22591970.20273090328790
1.8419-1.86430.24332030.18373120332391
1.8643-1.88790.2072380.17643133337191
1.8879-1.91280.2181990.17163130332991
1.9128-1.9390.20811930.1833158335192
1.939-1.96670.19162200.16483201342194
1.9667-1.9960.18322090.1523299350894
1.996-2.02720.17612070.1443237344495
2.0272-2.06050.17882170.14473295351296
2.0605-2.0960.1681870.13933345353296
2.096-2.13410.15912020.13683331353396
2.1341-2.17510.1652360.13223324356097
2.1751-2.21950.16972330.13153356358997
2.2195-2.26780.16372120.13673334354697
2.2678-2.32050.15362110.12793405361698
2.3205-2.37860.15821990.12933399359898
2.3786-2.44290.16062270.13673383361098
2.4429-2.51480.17282050.13423408361399
2.5148-2.59590.17462390.13763428366799
2.5959-2.68870.15942050.13513425363099
2.6887-2.79630.16552510.1413424367599
2.7963-2.92350.17062370.13833418365599
2.9235-3.07760.17282260.140434493675100
3.0776-3.27040.16192300.138234473677100
3.2704-3.52280.15172170.132134543671100
3.5228-3.87710.15642240.125134933717100
3.8771-4.43750.132380.113334773715100
4.4375-5.58870.1472040.122434993703100
5.5887-41.88760.1552330.15213537377099
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)
18.11011.69191.36252.2560.69182.1410.0035-0.22020.42590.10340.0565-0.0444-0.17020.0956-0.050.2053-0.02160.02310.1295-0.0150.173-25.7224-14.8464-32.2433
21.6215-0.1388-0.55632.0048-0.1661.42930.0312-0.21760.05830.25830.08090.0373-0.0751-0.0358-0.11760.2047-0.01270.02710.2117-0.02260.1543-31.2492-20.4856-27.2127
32.8197-0.0727-0.36292.84850.27363.71070.0752-0.47990.04430.365-0.0044-0.1520.04150.2091-0.06170.186-0.0228-0.04730.2966-0.04340.1757-16.5722-24.2613-25.0239
40.61320.05590.21740.62940.12860.7873-0.015-0.02970.0392-0.04060.00510.03840.0201-0.03070.0160.1669-0.01570.01320.1674-0.00240.1675-31.6646-28.6062-48.475
50.5032-0.08620.0250.8146-0.66731.4384-0.0394-0.0232-0.0896-0.01630.00740.14710.2426-0.19450.0190.2123-0.07310.01120.2035-0.01820.2152-43.8862-43.4549-45.1814
61.78320.4289-0.05382.35490.48522.3803-0.0259-0.106-0.20220.11160.0054-0.09520.34120.0280.02110.1964-0.00290.0160.16760.02490.191-28.067-42.651-37.3788
71.0020.0304-0.07790.40840.01731.2972-0.0308-0.087-0.01350.05170.00920.00970.02860.1210.0130.1756-0.03210.01260.20120.00110.1791-25.8926-32.0178-42.7085
83.0858-0.262-1.59162.6474-0.66242.27380.04950.01210.0069-0.2436-0.0829-0.13060.01390.11160.01350.1337-0.0281-0.03520.1626-0.00180.0866-26.5212-29.5181-54.0617
98.81146.4458-1.39354.8068-0.78220.9356-0.09470.0843-0.0277-0.3180.1892-0.1956-0.06260.0548-0.0360.210.00230.02840.1379-0.02050.2471-28.0708-10.5941-57.9083
100.45170.10760.06562.06370.66521.39140.04490.13820.0732-0.38840.01890.1002-0.0781-0.1522-0.05160.3109-0.0135-0.00450.21120.00070.238-35.6212-11.4376-63.1727
110.69760.1576-0.02421.28710.46671.2341-0.04180.05020.014-0.18870.03860.0813-0.0941-0.1456-0.01490.25830.0155-0.00250.16720.00270.2241-36.4292-1.2285-51.7375
126.41346.80092.27418.7872.62163.70350.2321-0.5335-0.13180.4142-0.25850.17150.1477-0.34030.01320.27640.0010.07330.33190.00520.2877-49.1159-14.9695-31.3981
131.4876-0.16790.15312.3821-0.59071.8378-0.00220.07370.1046-0.1208-0.03640.7909-0.139-0.5919-0.00170.25930.0207-0.01570.5016-0.03860.5427-61.4105-6.1205-45.1742
140.67910.1413-0.13452.31170.26141.7108-0.02040.03560.0705-0.1962-0.0380.3827-0.2927-0.24760.04690.26120.026-0.02280.2281-0.0140.2551-45.13192.7641-49.9922
151.9946-0.04351.87013.54970.07572.5153-0.2236-0.16150.16380.36340.07040.1828-0.2054-0.21440.11080.22830.00430.04540.19880.00340.1809-39.714-1.4429-36.1403
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1chain 'A' and (resid 3 through 29 )A3 - 29
2X-RAY DIFFRACTION2chain 'A' and (resid 30 through 75 )A30 - 75
3X-RAY DIFFRACTION3chain 'A' and (resid 76 through 109 )A76 - 109
4X-RAY DIFFRACTION4chain 'A' and (resid 110 through 197 )A110 - 197
5X-RAY DIFFRACTION5chain 'A' and (resid 198 through 301 )A198 - 301
6X-RAY DIFFRACTION6chain 'A' and (resid 302 through 341 )A302 - 341
7X-RAY DIFFRACTION7chain 'A' and (resid 342 through 392 )A342 - 392
8X-RAY DIFFRACTION8chain 'A' and (resid 393 through 424 )A393 - 424
9X-RAY DIFFRACTION9chain 'B' and (resid 3 through 29 )B3 - 29
10X-RAY DIFFRACTION10chain 'B' and (resid 30 through 75 )B30 - 75
11X-RAY DIFFRACTION11chain 'B' and (resid 76 through 176 )B76 - 176
12X-RAY DIFFRACTION12chain 'B' and (resid 177 through 197 )B177 - 197
13X-RAY DIFFRACTION13chain 'B' and (resid 198 through 301 )B198 - 301
14X-RAY DIFFRACTION14chain 'B' and (resid 302 through 392 )B302 - 392
15X-RAY DIFFRACTION15chain 'B' and (resid 393 through 424 )B393 - 424

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