[English] 日本語
Yorodumi
- PDB-3now: UNC-45 from Drosophila melanogaster -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 3now
TitleUNC-45 from Drosophila melanogaster
ComponentsUNC-45 protein, SD10334p
KeywordsPROTEIN BINDING / Armadillo Repeat / Hsp90 / Myosin / Tetra-tricopeptide Repeat / TPR / binding protein required for myosin function
Function / homology
Function and homology information


somatic muscle development / myosin filament assembly / muscle organ development / chaperone-mediated protein folding / negative regulation of innate immune response / Hsp90 protein binding / cellular response to heat / defense response to Gram-negative bacterium / cell differentiation / cytoplasm
Similarity search - Function
UNC-45/Cro1/She4, central domain / Myosin-binding striated muscle assembly central / : / Tetratricopeptide repeat / Leucine-rich Repeat Variant / Leucine-rich Repeat Variant / TPR repeat region circular profile. / TPR repeat profile. / Tetratricopeptide repeats / Tetratricopeptide repeat ...UNC-45/Cro1/She4, central domain / Myosin-binding striated muscle assembly central / : / Tetratricopeptide repeat / Leucine-rich Repeat Variant / Leucine-rich Repeat Variant / TPR repeat region circular profile. / TPR repeat profile. / Tetratricopeptide repeats / Tetratricopeptide repeat / Armadillo-like helical / Alpha Horseshoe / Tetratricopeptide-like helical domain superfamily / Armadillo-type fold / Mainly Alpha
Similarity search - Domain/homology
Biological speciesDrosophila melanogaster (fruit fly)
MethodX-RAY DIFFRACTION / SYNCHROTRON / SAD / Resolution: 2.992 Å
AuthorsLee, C.F. / Hauenstein, A.V. / Fleming, J.K. / Gasper, W.C. / Engelke, V. / Banumathi, S. / Bernstein, S.I. / Huxford, T.
CitationJournal: Structure / Year: 2011
Title: X-ray Crystal Structure of the UCS Domain-Containing UNC-45 Myosin Chaperone from Drosophila melanogaster.
Authors: Lee, C.F. / Hauenstein, A.V. / Fleming, J.K. / Gasper, W.C. / Engelke, V. / Sankaran, B. / Bernstein, S.I. / Huxford, T.
History
DepositionJun 25, 2010Deposition site: RCSB / Processing site: RCSB
Revision 1.0Mar 16, 2011Provider: repository / Type: Initial release
Revision 1.1Jul 13, 2011Group: Version format compliance
Revision 1.2Dec 27, 2023Group: Data collection / Database references / Category: chem_comp_atom / chem_comp_bond / database_2
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession

-
Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

-
Assembly

Deposited unit
A: UNC-45 protein, SD10334p


Theoretical massNumber of molelcules
Total (without water)89,8141
Polymers89,8141
Non-polymers00
Water0
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
2
A: UNC-45 protein, SD10334p

A: UNC-45 protein, SD10334p

A: UNC-45 protein, SD10334p


Theoretical massNumber of molelcules
Total (without water)269,4413
Polymers269,4413
Non-polymers00
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation8_555-z,x,-y1
crystal symmetry operation11_555y,-z,-x1
Buried area7000 Å2
ΔGint-38 kcal/mol
Surface area100150 Å2
MethodPISA
Unit cell
Length a, b, c (Å)184.079, 184.079, 184.079
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number195
Space group name H-MP23

-
Components

#1: Protein UNC-45 protein, SD10334p


Mass: 89813.523 Da / Num. of mol.: 1 / Fragment: UNP residues 138-947
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Drosophila melanogaster (fruit fly) / Gene: CG2708, Tom34 / Plasmid: pET16b / Production host: Escherichia coli (E. coli) / Strain (production host): Rosetta (DE3) pLysS / References: UniProt: Q960B1

-
Experimental details

-
Experiment

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

-
Sample preparation

CrystalDensity Matthews: 5.79 Å3/Da / Density % sol: 78.7 %
Crystal growTemperature: 291 K / Method: vapor diffusion, hanging drop / pH: 5.6
Details: 0.1 M sodium citrate, 0.2 M ammonium acetate, 25% (w/v) PEG 4000, 1% (v/v) ethylene glycol, pH 5.6, VAPOR DIFFUSION, HANGING DROP, temperature 291.0K

-
Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: ALS / Beamline: 8.2.2 / Wavelength: 1 Å
DetectorType: ADSC QUANTUM 315 / Detector: CCD / Date: Aug 10, 2007
RadiationScattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 2.992→50 Å / Num. obs: 42099 / % possible obs: 99.8 % / Observed criterion σ(F): 2 / Observed criterion σ(I): 2 / Redundancy: 9.5 % / Rsym value: 0.0115 / Net I/σ(I): 19.2
Reflection shellResolution: 2.992→3.11 Å / Redundancy: 6.5 % / Num. unique all: 4113 / % possible all: 97.8

-
Processing

Software
NameVersionClassification
HKL-2000data collection
PHENIX(phenix.refine: 1.5_2)model building
PHENIX(phenix.refine: 1.5_2)refinement
HKL-2000data reduction
HKL-2000data scaling
PHENIX1.5_2phasing
RefinementMethod to determine structure: SAD / Resolution: 2.992→49.197 Å / SU ML: 0.45 / σ(F): 0.15 / Stereochemistry target values: ML
RfactorNum. reflection% reflectionSelection details
Rfree0.2355 1865 4.74 %random
Rwork0.2007 ---
obs0.2024 39354 93.27 %-
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL / Bsol: 20.07 Å2 / ksol: 0.292 e/Å3
Displacement parameters
Baniso -1Baniso -2Baniso -3
1-0 Å20 Å20 Å2
2---0 Å2-0 Å2
3---0 Å2
Refinement stepCycle: LAST / Resolution: 2.992→49.197 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms6077 0 0 0 6077
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0136145
X-RAY DIFFRACTIONf_angle_d1.2938296
X-RAY DIFFRACTIONf_dihedral_angle_d17.6142309
X-RAY DIFFRACTIONf_chiral_restr0.082992
X-RAY DIFFRACTIONf_plane_restr0.0041064
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2.9917-3.09860.3511530.29983183X-RAY DIFFRACTION79
3.0986-3.22260.31521720.28183432X-RAY DIFFRACTION87
3.2226-3.36930.3031740.26063628X-RAY DIFFRACTION91
3.3693-3.54680.28371830.23263697X-RAY DIFFRACTION93
3.5468-3.7690.28161870.20863782X-RAY DIFFRACTION95
3.769-4.05990.23521930.18193815X-RAY DIFFRACTION96
4.0599-4.46820.19971980.16223891X-RAY DIFFRACTION97
4.4682-5.11420.17091990.15473929X-RAY DIFFRACTION97
5.1142-6.4410.22751960.18113994X-RAY DIFFRACTION98
6.441-49.20380.18152100.16584138X-RAY DIFFRACTION99

+
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