[English] 日本語
Yorodumi
- PDB-5bwd: Benzylsuccinate alpha-gamma bound to fumarate -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 5bwd
TitleBenzylsuccinate alpha-gamma bound to fumarate
Components(benzylsuccinate synthase ...) x 2
KeywordsLYASE / complex / radical / disorder
Function / homology
Function and homology information


Benzylsuccinate synthase gamma subunit / Benzylsuccinate synthase gamma subunit superfamily / BssC/TutF protein / : / Formate C-acetyltransferase glycine radical, conserved site / Glycine radical domain signature. / Pyruvate formate lyase domain / Pyruvate formate lyase-like / Pyruvate formate-lyase domain profile. / Glycine radical ...Benzylsuccinate synthase gamma subunit / Benzylsuccinate synthase gamma subunit superfamily / BssC/TutF protein / : / Formate C-acetyltransferase glycine radical, conserved site / Glycine radical domain signature. / Pyruvate formate lyase domain / Pyruvate formate lyase-like / Pyruvate formate-lyase domain profile. / Glycine radical / Glycine radical domain / Glycine radical domain profile.
Similarity search - Domain/homology
FUMARIC ACID / TRIETHYLENE GLYCOL / TutF / TutD
Similarity search - Component
Biological speciesThauera aromatica (bacteria)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2 Å
AuthorsFunk, M.A. / Drennan, C.L.
Funding support United States, 2items
OrganizationGrant numberCountry
National Science Foundation (NSF, United States)0645960 United States
Howard Hughes Medical Institute (HHMI) United States
CitationJournal: J.Biol.Chem. / Year: 2015
Title: Substrate-bound Structures of Benzylsuccinate Synthase Reveal How Toluene Is Activated in Anaerobic Hydrocarbon Degradation.
Authors: Funk, M.A. / Marsh, E.N. / Drennan, C.L.
History
DepositionJun 7, 2015Deposition site: RCSB / Processing site: RCSB
Revision 1.0Aug 5, 2015Provider: repository / Type: Initial release
Revision 1.1Aug 12, 2015Group: Database references
Revision 1.2Sep 23, 2015Group: Database references
Revision 1.3Sep 6, 2017Group: Author supporting evidence / Database references / Derived calculations
Category: citation / pdbx_audit_support / pdbx_struct_oper_list
Item: _citation.journal_id_CSD / _pdbx_audit_support.funding_organization / _pdbx_struct_oper_list.symmetry_operation
Revision 1.4Nov 20, 2019Group: Author supporting evidence / Category: pdbx_audit_support / Item: _pdbx_audit_support.funding_organization
Revision 1.5Sep 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
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession
Revision 2.0Nov 15, 2023Group: Atomic model / Data collection / Category: atom_site / chem_comp_atom / chem_comp_bond
Item: _atom_site.auth_atom_id / _atom_site.label_atom_id ..._atom_site.auth_atom_id / _atom_site.label_atom_id / _chem_comp_atom.atom_id / _chem_comp_bond.atom_id_1 / _chem_comp_bond.atom_id_2

-
Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

-
Assembly

Deposited unit
A: benzylsuccinate synthase alpha chain
C: benzylsuccinate synthase gamma chain
hetero molecules


Theoretical massNumber of molelcules
Total (without water)107,16610
Polymers105,9832
Non-polymers1,1838
Water7,458414
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area3740 Å2
ΔGint18 kcal/mol
Surface area31490 Å2
MethodPISA
Unit cell
Length a, b, c (Å)154.862, 154.862, 82.117
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number96
Space group name H-MP43212

-
Components

-
Benzylsuccinate synthase ... , 2 types, 2 molecules AC

#1: Protein benzylsuccinate synthase alpha chain / tutD


Mass: 99117.109 Da / Num. of mol.: 1 / Mutation: M789I
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Thauera aromatica (bacteria) / Strain: T1 / Gene: tutD / Plasmid: pETDuet / Production host: Escherichia coli BL21(DE3) (bacteria) / References: UniProt: O68395, benzylsuccinate synthase
#2: Protein benzylsuccinate synthase gamma chain / TutF


Mass: 6865.687 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Thauera aromatica (bacteria) / Strain: T1 / Gene: tutF / Plasmid: pETDuet / Production host: Escherichia coli BL21(DE3) (bacteria) / References: UniProt: O68394

-
Non-polymers , 5 types, 422 molecules

#3: Chemical ChemComp-FUM / FUMARIC ACID


Mass: 116.072 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C4H4O4
#4: Chemical ChemComp-TRS / 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL / TRIS BUFFER


Mass: 122.143 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C4H12NO3 / Comment: pH buffer*YM
#5: Chemical
ChemComp-PGE / TRIETHYLENE GLYCOL


Mass: 150.173 Da / Num. of mol.: 5 / Source method: obtained synthetically / Formula: C6H14O4
#6: Chemical ChemComp-PG4 / TETRAETHYLENE GLYCOL


Mass: 194.226 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Formula: C8H18O5 / Comment: precipitant*YM
#7: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 414 / Source method: isolated from a natural source / Formula: H2O

-
Experimental details

-
Experiment

ExperimentMethod: X-RAY DIFFRACTION

-
Sample preparation

CrystalDensity Matthews: 2.38 Å3/Da / Density % sol: 48.22 %
Description: Pale yellow and three-dimensional with rounded edges and facets. Some cabochon-like crystals with no apparent facets. Crystal morphology is pH-dependent.
Crystal growTemperature: 291 K / Method: vapor diffusion
Details: 1:1 15 mg/mL BSS-alpha-gamma (in 20 mM HEPES, pH 7.6, 100 mM sodium chloride, 5 mM fumarate) to well solution (20% w/v PEG400, 50 mM Bis-Tris, pH 6.5, 25 mM Tris, pH 8.0) in temperature- ...Details: 1:1 15 mg/mL BSS-alpha-gamma (in 20 mM HEPES, pH 7.6, 100 mM sodium chloride, 5 mM fumarate) to well solution (20% w/v PEG400, 50 mM Bis-Tris, pH 6.5, 25 mM Tris, pH 8.0) in temperature-controlled anaerobic chamber, crystals formed in several days
PH range: 6.5-8.0

-
Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: NSLS / Beamline: X26C / Wavelength: 1 Å
DetectorType: ADSC QUANTUM 315r / Detector: CCD / Date: Jul 19, 2011
RadiationMonochromator: Si(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 2→35 Å / Num. obs: 65770 / % possible obs: 97 % / Redundancy: 5.6 % / Biso Wilson estimate: 32.19 Å2 / Rsym value: 0.085 / Net I/σ(I): 11.8
Reflection shellResolution: 2→2.03 Å / Redundancy: 2.8 % / Rmerge(I) obs: 0.9 / Mean I/σ(I) obs: 1.4 / % possible all: 80.4

-
Processing

Software
NameVersionClassification
PHENIXdev_1951refinement
HKL-2000data reduction
HKL-2000data scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB entry 4PKC
Resolution: 2→34.628 Å / SU ML: 0.25 / Cross valid method: FREE R-VALUE / σ(F): 1.34 / Phase error: 27.75 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2232 3271 4.99 %
Rwork0.1951 --
obs0.1965 65615 96.9 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.2 Å / Solvent model: FLAT BULK SOLVENT MODEL
Refinement stepCycle: LAST / Resolution: 2→34.628 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms7056 0 79 414 7549
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0037301
X-RAY DIFFRACTIONf_angle_d0.7059838
X-RAY DIFFRACTIONf_dihedral_angle_d11.9842760
X-RAY DIFFRACTIONf_chiral_restr0.0331028
X-RAY DIFFRACTIONf_plane_restr0.0031285
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2-2.02990.39971090.35352202X-RAY DIFFRACTION80
2.0299-2.06160.35211150.31262303X-RAY DIFFRACTION83
2.0616-2.09540.27831290.30152373X-RAY DIFFRACTION87
2.0954-2.13150.37531280.2792487X-RAY DIFFRACTION90
2.1315-2.17030.28731380.26292576X-RAY DIFFRACTION93
2.1703-2.2120.311440.24382718X-RAY DIFFRACTION99
2.212-2.25710.27851450.2222762X-RAY DIFFRACTION100
2.2571-2.30620.2691430.20532767X-RAY DIFFRACTION100
2.3062-2.35980.22981480.2022752X-RAY DIFFRACTION100
2.3598-2.41880.25141470.20252769X-RAY DIFFRACTION100
2.4188-2.48420.23151450.1972770X-RAY DIFFRACTION100
2.4842-2.55730.24461450.20222765X-RAY DIFFRACTION100
2.5573-2.63980.22691460.19432786X-RAY DIFFRACTION100
2.6398-2.73410.28381470.20292774X-RAY DIFFRACTION100
2.7341-2.84360.26371460.20182780X-RAY DIFFRACTION100
2.8436-2.97290.25051480.2072798X-RAY DIFFRACTION100
2.9729-3.12950.21761480.20922792X-RAY DIFFRACTION100
3.1295-3.32550.25131470.20892804X-RAY DIFFRACTION100
3.3255-3.5820.20671470.18492811X-RAY DIFFRACTION100
3.582-3.9420.20151490.1712819X-RAY DIFFRACTION100
3.942-4.51140.16361490.15252841X-RAY DIFFRACTION100
4.5114-5.67980.18361520.16682883X-RAY DIFFRACTION100
5.6798-34.63340.18771560.18423012X-RAY DIFFRACTION99
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)
10.4560.13390.26090.43110.21710.18240.26930.2026-0.2710.0358-0.0076-0.38840.27560.40490.54130.30950.2294-0.05240.5294-0.19380.736720.2604-62.2678-15.0094
20.8677-0.34230.08650.61560.00230.1628-0.0075-0.0794-0.1546-0.00840.02770.04210.0274-0.0254-00.2474-0.0025-0.01940.2590.01620.2526-12.3147-41.69632.3042
30.2434-0.0287-0.16970.2935-0.09570.10630.00310.0277-0.0175-0.13240.0355-0.11990.01280.0465-00.27210.0133-0.03310.29150.00330.31243.9793-48.24761.3658
40.397-0.19530.32070.2130.17040.6330.05240.1550.1315-0.1039-0.0455-0.3927-0.05310.228100.28440.01260.06230.37950.02320.36917.7912-36.8672-11.7799
50.06470.12010.06980.21320.13380.0711-0.03780.01740.0721-0.0821-0.0053-0.1756-0.1290.0005-00.3254-0.00740.04970.3050.05640.2969-7.4639-23.4903-19.281
60.29930.03740.21680.10120.05340.12660.09920.1344-0.0214-0.0723-0.059-0.28130.0570.20040.01310.32960.05880.05690.3586-0.00590.3748-0.0175-28.7699-12.9986
70.04280.0259-0.01780.0569-0.00780.00380.00080.1551-0.0265-0.2439-0.1492-0.0812-0.13250.0907-0.02641.2469-0.04070.20161.3006-0.03240.31262.4864-31.0595-49.7893
80.0903-0.12910.06910.1846-0.0960.0497-0.19890.06070.0054-0.0837-0.0037-0.0475-0.02530.0054-0.01791.12780.25650.18981.5933-0.41970.73534.3386-40.5678-48.1252
90.1950.097-0.0890.2842-0.31620.3402-0.10930.39620.2011-0.1471-0.1611-0.41140.05760.4602-0.46140.36640.05430.25240.68840.09050.40678.7369-26.6463-25.8786
100.0043-0.0027-0.00240.0054-0.00340.00250.01540.0784-0.02940.06560.07310.02720.06170.0899-0.00010.86630.08940.11030.7173-0.16260.4948-0.764-38.7904-36.4111
110.0035-0.00260.00160.00160.00030.00240.04130.0449-0.07130.0216-0.01160.00860.02170.0017-01.03540.2569-0.15770.9802-0.27720.67070.7118-43.512-38.0171
120.1228-0.0194-0.10230.03460.01790.0581-0.01870.4849-0.0392-0.15070.0218-0.3044-0.13860.30290.12090.68910.08430.22131.0887-0.06420.831919.0181-41.4774-23.2013
130.0414-0.00050.03520.0041-0.0110.05590.0860.27090.2098-0.07490.1435-0.020.04490.1020.07580.410.08830.12411.0365-0.03380.58225.5645-42.8231-15.461
140.48630.00380.44950.2619-0.01580.48970.0540.46590.0004-0.3099-0.22680.04610.20060.3414-0.32120.51090.14640.05940.749-0.26640.434112.7853-51.8971-22.4379
150.0158-0.0046-0.02580.0107-0.00010.06510.08870.1166-0.33350.0778-0.06290.0094-0.09280.1845-0.00030.45970.1674-0.05320.5369-0.17670.52124.0434-58.4957-18.8236
160.0018-0.00740.0010.0165-0.00590.0303-0.0020.1670.1455-0.1463-0.1033-0.317-0.23040.2489-00.89480.2251-0.03291.2019-0.05060.634411.587-52.0583-28.5578
170.0032-0.00570.00220.0066-0.00080.00040.06360.06920.10110.0023-0.00510.0065-0.0066-0.050300.80430.24210.25831.34040.07311.409132.9045-43.5813-22.4942
180.03160.0057-0.00160.0066-0.00950.0084-0.06990.0061-0.1002-0.04810.00840.2252-0.0073-0.4472-0.00010.4486-0.06460.11340.52290.10620.5729-19.8211-53.162920.288
190.0585-0.00250.05460.02840.00150.05840.146-0.0647-0.513-0.08610.20220.08770.1219-0.15970.010.35640.0005-0.01020.31830.07960.5975-16.0066-61.66796.9792
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1chain 'A' and (resseq 6:52)
2X-RAY DIFFRACTION2chain 'A' and (resseq 53:321)
3X-RAY DIFFRACTION3chain 'A' and (resseq 322:385)
4X-RAY DIFFRACTION4chain 'A' and (resseq 386:546)
5X-RAY DIFFRACTION5chain 'A' and (resseq 555:583)
6X-RAY DIFFRACTION6chain 'A' and (resseq 584:634)
7X-RAY DIFFRACTION7chain 'A' and (resseq 635:650)
8X-RAY DIFFRACTION8chain 'A' and (resseq 651:663)
9X-RAY DIFFRACTION9chain 'A' and (resseq 664:708)
10X-RAY DIFFRACTION10chain 'A' and (resseq 716:725)
11X-RAY DIFFRACTION11chain 'A' and (resseq 726:731)
12X-RAY DIFFRACTION12chain 'A' and (resseq 744:780)
13X-RAY DIFFRACTION13chain 'A' and (resseq 781:794)
14X-RAY DIFFRACTION14chain 'A' and (resseq 795:815)
15X-RAY DIFFRACTION15chain 'A' and (resseq 816:838)
16X-RAY DIFFRACTION16chain 'A' and (resseq 839:854)
17X-RAY DIFFRACTION17chain 'A' and (resseq 855:865)
18X-RAY DIFFRACTION18chain 'C' and (resseq 9:26)
19X-RAY DIFFRACTION19chain 'C' and (resseq 27:47)

+
About Yorodumi

-
News

-
Feb 9, 2022. New format data for meta-information of EMDB entries

New format data for meta-information of EMDB entries

  • Version 3 of the EMDB header file is now the official format.
  • The previous official version 1.9 will be removed from the archive.

Related info.:EMDB header

External links:wwPDB to switch to version 3 of the EMDB data model

-
Aug 12, 2020. Covid-19 info

Covid-19 info

URL: https://pdbj.org/emnavi/covid19.php

New page: Covid-19 featured information page in EM Navigator.

Related info.:Covid-19 info / Mar 5, 2020. Novel coronavirus structure data

+
Mar 5, 2020. Novel coronavirus structure data

Novel coronavirus structure data

Related info.:Yorodumi Speices / Aug 12, 2020. Covid-19 info

External links:COVID-19 featured content - PDBj / Molecule of the Month (242):Coronavirus Proteases

+
Jan 31, 2019. EMDB accession codes are about to change! (news from PDBe EMDB page)

EMDB accession codes are about to change! (news from PDBe EMDB page)

  • The allocation of 4 digits for EMDB accession codes will soon come to an end. Whilst these codes will remain in use, new EMDB accession codes will include an additional digit and will expand incrementally as the available range of codes is exhausted. The current 4-digit format prefixed with “EMD-” (i.e. EMD-XXXX) will advance to a 5-digit format (i.e. EMD-XXXXX), and so on. It is currently estimated that the 4-digit codes will be depleted around Spring 2019, at which point the 5-digit format will come into force.
  • The EM Navigator/Yorodumi systems omit the EMD- prefix.

Related info.:Q: What is EMD? / ID/Accession-code notation in Yorodumi/EM Navigator

External links:EMDB Accession Codes are Changing Soon! / Contact to PDBj

+
Jul 12, 2017. Major update of PDB

Major update of PDB

  • wwPDB released updated PDB data conforming to the new PDBx/mmCIF dictionary.
  • This is a major update changing the version number from 4 to 5, and with Remediation, in which all the entries are updated.
  • In this update, many items about electron microscopy experimental information are reorganized (e.g. em_software).
  • Now, EM Navigator and Yorodumi are based on the updated data.

External links:wwPDB Remediation / Enriched Model Files Conforming to OneDep Data Standards Now Available in the PDB FTP Archive

-
Yorodumi

Thousand views of thousand structures

  • Yorodumi is a browser for structure data from EMDB, PDB, SASBDB, etc.
  • This page is also the successor to EM Navigator detail page, and also detail information page/front-end page for Omokage search.
  • The word "yorodu" (or yorozu) is an old Japanese word meaning "ten thousand". "mi" (miru) is to see.

Related info.:EMDB / PDB / SASBDB / Comparison of 3 databanks / Yorodumi Search / Aug 31, 2016. New EM Navigator & Yorodumi / Yorodumi Papers / Jmol/JSmol / Function and homology information / Changes in new EM Navigator and Yorodumi

Read more