[English] 日本語
Yorodumi
- PDB-1svi: Crystal Structure of the GTP-binding protein YsxC complexed with GDP -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 1svi
TitleCrystal Structure of the GTP-binding protein YsxC complexed with GDP
ComponentsGTP-binding protein YSXC
KeywordsHYDROLASE / YsxC / ENGB / GTPase / GTP-binding protein / GDP
Function / homology
Function and homology information


division septum assembly / GTP binding / metal ion binding / cytosol
Similarity search - Function
GTP-binding protein, ribosome biogenesis, YsxC / EngB-type guanine nucleotide-binding (G) domain profile. / EngB-type guanine nucleotide-binding (G) domain / 50S ribosome-binding GTPase / GTP binding domain / Small GTP-binding protein domain / P-loop containing nucleotide triphosphate hydrolases / P-loop containing nucleoside triphosphate hydrolase / Rossmann fold / 3-Layer(aba) Sandwich / Alpha Beta
Similarity search - Domain/homology
GUANOSINE-5'-DIPHOSPHATE / Probable GTP-binding protein EngB
Similarity search - Component
Biological speciesBacillus subtilis (bacteria)
MethodX-RAY DIFFRACTION / MIR / Resolution: 1.95 Å
AuthorsRuzheinikov, S.N. / Das, S.K. / Sedelnikova, S.E. / Baker, P.J. / Artymiuk, P.J. / Garcia-Lara, J. / Foster, S.J. / Rice, D.W.
Citation
Journal: J.Mol.Biol. / Year: 2004
Title: Analysis of the Open and Closed Conformations of the GTP-binding Protein YsxC from Bacillus subtilis.
Authors: Ruzheinikov, S.N. / Das, S.K. / Sedelnikova, S.E. / Baker, P.J. / Artymiuk, P.J. / Garcia-Lara, J. / Foster, S.J. / Rice, D.W.
#1: Journal: To be Published
Title: Expression, purification, crystallization and preliminary crystallographic analysis of a putative GTP-binding protein, YsxC, from Bacillus subtilis .
Authors: Das, S.K. / Sedelnikova, S.E. / Baker, P.J. / Ruzheinikov, S.N. / Foster, S.J. / Rice, D.W.
History
DepositionMar 29, 2004Deposition site: RCSB / Processing site: RCSB
Revision 1.0May 25, 2004Provider: repository / Type: Initial release
Revision 1.1Apr 30, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Oct 11, 2017Group: Refinement description / Category: software / Item: _software.classification / _software.name
Revision 1.4Feb 14, 2024Group: Data collection / Database references / Derived calculations
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / struct_site
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id

-
Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

-
Assembly

Deposited unit
A: GTP-binding protein YSXC
hetero molecules


Theoretical massNumber of molelcules
Total (without water)22,5042
Polymers22,0601
Non-polymers4431
Water4,432246
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)46.179, 68.305, 61.999
Angle α, β, γ (deg.)90.00, 94.05, 90.00
Int Tables number5
Space group name H-MC121

-
Components

#1: Protein GTP-binding protein YSXC


Mass: 22060.414 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Bacillus subtilis (bacteria) / Gene: YsxC, ENGB, BSU28190 / Production host: Escherichia coli (E. coli) / References: UniProt: P38424
#2: Chemical ChemComp-GDP / GUANOSINE-5'-DIPHOSPHATE / Guanosine diphosphate


Type: RNA linking / Mass: 443.201 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C10H15N5O11P2 / Comment: GDP, energy-carrying molecule*YM
#3: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 246 / Source method: isolated from a natural source / Formula: H2O

-
Experimental details

-
Experiment

ExperimentMethod: X-RAY DIFFRACTION / Number of used crystals: 1

-
Sample preparation

CrystalDensity Matthews: 2.21 Å3/Da / Density % sol: 44.34 %
Crystal growTemperature: 290 K / Method: vapor diffusion, hanging drop / pH: 7.5
Details: PG 4000, isopropanol, N Hepes buffer, GDP,MgCl2, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 290K

-
Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: ROTATING ANODE / Type: RIGAKU RU200 / Wavelength: 1.5418 Å
DetectorType: MARRESEARCH / Detector: IMAGE PLATE / Date: Jan 1, 2002
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.5418 Å / Relative weight: 1
ReflectionResolution: 1.95→10 Å / Num. obs: 13194 / % possible obs: 94.8 % / Observed criterion σ(F): 2 / Observed criterion σ(I): 2

-
Processing

Software
NameVersionClassification
REFMAC5refinement
MAR345data collection
SCALEPACKdata scaling
MLPHAREphasing
RefinementMethod to determine structure: MIR / Resolution: 1.95→10 Å / Cor.coef. Fo:Fc: 0.957 / Cor.coef. Fo:Fc free: 0.934 / SU B: 4.265 / SU ML: 0.122 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.199 / ESU R Free: 0.167 / Stereochemistry target values: MAXIMUM LIKELIHOOD
RfactorNum. reflection% reflectionSelection details
Rfree0.22174 641 4.9 %RANDOM
Rwork0.17614 ---
obs0.17831 12485 94.13 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: BABINET MODEL WITH MASK
Displacement parametersBiso mean: 17.442 Å2
Baniso -1Baniso -2Baniso -3
1-0.34 Å20 Å2-0.58 Å2
2---0.53 Å20 Å2
3---0.11 Å2
Refinement stepCycle: LAST / Resolution: 1.95→10 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms1457 0 28 246 1731
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0080.0221515
X-RAY DIFFRACTIONr_angle_refined_deg1.2871.9822049
X-RAY DIFFRACTIONr_dihedral_angle_1_deg3.3973180
X-RAY DIFFRACTIONr_dihedral_angle_3_deg17.49415291
X-RAY DIFFRACTIONr_chiral_restr0.0890.2227
X-RAY DIFFRACTIONr_gen_planes_refined0.0040.021104
X-RAY DIFFRACTIONr_nbd_refined0.2350.3774
X-RAY DIFFRACTIONr_xyhbond_nbd_refined0.2140.5197
X-RAY DIFFRACTIONr_symmetry_vdw_refined0.2310.343
X-RAY DIFFRACTIONr_symmetry_hbond_refined0.630.522
X-RAY DIFFRACTIONr_mcbond_it0.5471.5906
X-RAY DIFFRACTIONr_mcangle_it1.06121471
X-RAY DIFFRACTIONr_scbond_it1.7913609
X-RAY DIFFRACTIONr_scangle_it3.0314.5578
LS refinement shellResolution: 1.95→1.999 Å / Total num. of bins used: 20 /
RfactorNum. reflection
Rfree0.309 43
Rwork0.237 887
Refinement TLS params.Method: refined / Origin x: 10.415 Å / Origin y: 34.7705 Å / Origin z: 44.6358 Å
111213212223313233
T0.0227 Å20.03 Å2-0.0041 Å2-0.0406 Å20.0004 Å2--0.0437 Å2
L1.3004 °2-0.0941 °2-0.1497 °2-1.3124 °2-0.3525 °2--2.7536 °2
S-0.0025 Å °-0.0566 Å °0.0547 Å °0.149 Å °0.0837 Å °-0.0353 Å °-0.0936 Å °-0.2315 Å °-0.0812 Å °

+
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