[English] 日本語
Yorodumi
- PDB-5yu7: CRYSTAL STRUCTURE OF EXPORTIN-5 -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 5yu7
TitleCRYSTAL STRUCTURE OF EXPORTIN-5
ComponentsExportin-5
KeywordsRNA BINDING PROTEIN
Function / homology
Function and homology information


RISC complex binding / pre-miRNA binding / RNA nuclear export complex / pre-miRNA export from nucleus / nuclear export signal receptor activity / miRNA metabolic process / RISC complex / RNA export from nucleus / MicroRNA (miRNA) biogenesis / protein export from nucleus ...RISC complex binding / pre-miRNA binding / RNA nuclear export complex / pre-miRNA export from nucleus / nuclear export signal receptor activity / miRNA metabolic process / RISC complex / RNA export from nucleus / MicroRNA (miRNA) biogenesis / protein export from nucleus / small GTPase binding / tRNA binding / mRNA binding / RNA binding / nucleoplasm / nucleus / cytoplasm / cytosol
Similarity search - Function
Exportin-5, C-terminal domain / Exportin-5 family / Exportin-1/5 / Exportin-1/Importin-beta-like / Exportin 1-like protein / Importin-beta N-terminal domain / Importin-beta N-terminal domain / Importin-beta, N-terminal domain / Leucine-rich Repeat Variant / Leucine-rich Repeat Variant ...Exportin-5, C-terminal domain / Exportin-5 family / Exportin-1/5 / Exportin-1/Importin-beta-like / Exportin 1-like protein / Importin-beta N-terminal domain / Importin-beta N-terminal domain / Importin-beta, N-terminal domain / Leucine-rich Repeat Variant / Leucine-rich Repeat Variant / Armadillo-like helical / Alpha Horseshoe / Armadillo-type fold / Mainly Alpha
Similarity search - Domain/homology
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3.301 Å
AuthorsYamazawa, R. / Jiko, C. / Lee, S.J. / Yamashita, E.
Funding support Japan, Korea, Republic Of, 4items
OrganizationGrant numberCountry
MEXT22121006 Japan
JSPS22370041 Japan
JSPS21227003 Japan
NRFMEST 2011-0017405 Korea, Republic Of
CitationJournal: Structure / Year: 2018
Title: Structural Basis for Selective Binding of Export Cargoes by Exportin-5
Authors: Yamazawa, R. / Jiko, C. / Choi, S. / Park, I.Y. / Nakagawa, A. / Yamashita, E. / Lee, S.J.
History
DepositionNov 20, 2017Deposition site: PDBJ / Processing site: PDBJ
Revision 1.0Aug 29, 2018Provider: repository / Type: Initial release
Revision 1.1Oct 17, 2018Group: Data collection / Database references / Category: citation
Item: _citation.journal_volume / _citation.page_first / _citation.page_last
Revision 1.2Jul 7, 2021Group: Database references / Structure summary / Category: audit_author / citation_author
Item: _audit_author.identifier_ORCID / _citation_author.identifier_ORCID
Revision 1.3Nov 22, 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

-
Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

-
Assembly

Deposited unit
A: Exportin-5


Theoretical massNumber of molelcules
Total (without water)136,4551
Polymers136,4551
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author
  • Evidence: gel filtration
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area0 Å2
ΔGint0 kcal/mol
Surface area50580 Å2
Unit cell
Length a, b, c (Å)286.163, 286.163, 59.349
Angle α, β, γ (deg.)90.00, 90.00, 120.00
Int Tables number172
Space group name H-MP64

-
Components

#1: Protein Exportin-5 / Exp5 / Ran-binding protein 21


Mass: 136454.719 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: XPO5, KIAA1291, RANBP21 / Production host: Escherichia coli (E. coli) / References: UniProt: Q9HAV4

-
Experimental details

-
Experiment

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

-
Sample preparation

CrystalDensity Matthews: 5.14 Å3/Da / Density % sol: 76.07 %
Crystal growTemperature: 283 K / Method: vapor diffusion, hanging drop / Details: PEG3350, Tacsimate, MPD, MgCl2, DTT

-
Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: SPring-8 / Beamline: BL44XU / Wavelength: 0.9 Å
DetectorType: RAYONIX MX300HE / Detector: CCD / Date: Feb 2, 2015
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9 Å / Relative weight: 1
ReflectionResolution: 3.3→50 Å / Num. obs: 42325 / % possible obs: 99.5 % / Redundancy: 4.7 % / Rmerge(I) obs: 0.068 / Net I/σ(I): 28
Reflection shellResolution: 3.3→3.36 Å / Redundancy: 4.8 % / Rmerge(I) obs: 0.845 / Mean I/σ(I) obs: 1.9 / Num. unique obs: 2056 / % possible all: 100

-
Processing

Software
NameVersionClassification
PHENIX(1.11.1_2575: ???)refinement
HKL-2000data reduction
HKL-2000data scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 3A6P
Resolution: 3.301→41.304 Å / SU ML: 0.36 / Cross valid method: THROUGHOUT / σ(F): 1.36 / Phase error: 23.43 / Stereochemistry target values: ML
RfactorNum. reflection% reflectionSelection details
Rfree0.2292 2156 5.1 %RANDOM
Rwork0.1996 ---
obs0.2011 42295 99.48 %-
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Refinement stepCycle: LAST / Resolution: 3.301→41.304 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms8937 0 0 0 8937
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0029112
X-RAY DIFFRACTIONf_angle_d0.44212330
X-RAY DIFFRACTIONf_dihedral_angle_d9.5535582
X-RAY DIFFRACTIONf_chiral_restr0.0341420
X-RAY DIFFRACTIONf_plane_restr0.0031572
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
3.3007-3.37740.35181380.31372628X-RAY DIFFRACTION100
3.3774-3.46190.31281550.2872657X-RAY DIFFRACTION100
3.4619-3.55540.30641440.25512648X-RAY DIFFRACTION100
3.5554-3.660.26331540.23462663X-RAY DIFFRACTION100
3.66-3.7780.25171410.22242662X-RAY DIFFRACTION100
3.778-3.9130.24461420.20222684X-RAY DIFFRACTION100
3.913-4.06950.26671620.20512632X-RAY DIFFRACTION100
4.0695-4.25450.19351330.17722713X-RAY DIFFRACTION100
4.2545-4.47860.23151520.1832657X-RAY DIFFRACTION100
4.4786-4.75880.18781330.17452677X-RAY DIFFRACTION100
4.7588-5.12560.20881570.18082685X-RAY DIFFRACTION100
5.1256-5.64030.26661160.20572730X-RAY DIFFRACTION100
5.6403-6.45380.27861180.22562758X-RAY DIFFRACTION100
6.4538-8.12090.24271620.21252706X-RAY DIFFRACTION100
8.1209-41.30730.1871490.17322639X-RAY DIFFRACTION93
Refinement TLS params.Method: refined / Origin x: 121.8252 Å / Origin y: 41.236 Å / Origin z: -3.8069 Å
111213212223313233
T1.3847 Å2-0.0017 Å2-0.3483 Å2-0.7982 Å20.1041 Å2--1.0115 Å2
L2.2352 °2-1.504 °2-0.6245 °2-2.4257 °2-0.1146 °2--0.6133 °2
S-0.2062 Å °-0.0127 Å °1.0053 Å °0.1069 Å °0.4364 Å °-0.2684 Å °-0.3489 Å °-0.1843 Å °-0.2132 Å °
Refinement TLS groupSelection details: all

+
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://pdbjlvh1.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