[English] 日本語
Yorodumi
- PDB-8add: Viral tegument-like DUBs -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 8add
TitleViral tegument-like DUBs
ComponentsATP-dependent DNA helicase
KeywordsHYDROLASE / deubiquitinating enzyme / ubiquitin / tegument
Function / homology
Function and homology information


DNA helicase activity / telomere maintenance / DNA recombination / DNA helicase / DNA repair / ATP hydrolysis activity / ATP binding
Similarity search - Function
Helitron helicase-like domain / Domain of unknown function DUF6570 / Helitron helicase-like domain at N-terminus / Domain of unknown function (DUF6570) / DNA helicase Pif1-like / PIF1-like helicase / Herpesvirus large tegument protein, USP domain / Herpesvirus tegument protein, N-terminal conserved region / Endonuclease/exonuclease/phosphatase superfamily / Papain-like cysteine peptidase superfamily / P-loop containing nucleoside triphosphate hydrolase
Similarity search - Domain/homology
ATP-dependent DNA helicase
Similarity search - Component
Biological speciesDanio rerio (zebrafish)
MethodX-RAY DIFFRACTION / SYNCHROTRON / SIR / Resolution: 1.9 Å
AuthorsErven, I. / Abraham, E.T. / Hermanns, T. / Hofmann, K. / Baumann, U.
Funding support Germany, 2items
OrganizationGrant numberCountry
German Research Foundation (DFG)HO 3783/3-1 Germany
German Research Foundation (DFG)INST 216/949-1 FUGG Germany
Citation
Journal: Nat Commun / Year: 2022
Title: A widely distributed family of eukaryotic and bacterial deubiquitinases related to herpesviral large tegument proteins.
Authors: Erven, I. / Abraham, E. / Hermanns, T. / Baumann, U. / Hofmann, K.
#1: Journal: Nat Commun / Year: 2022
Title: A structural basis for the diverse linkage specificities within the ZUFSP deubiquitinase family.
Authors: Hermanns, T. / Pichlo, C. / Baumann, U. / Hofmann, K.
#2: Journal: Nat Commun / Year: 2018
Title: A family of unconventional deubiquitinases with modular chain specificity determinants.
Authors: Hermanns, T. / Pichlo, C. / Woiwode, I. / Klopffleisch, K. / Witting, K.F. / Ovaa, H. / Baumann, U. / Hofmann, K.
History
DepositionJul 8, 2022Deposition site: PDBE / Processing site: PDBE
Revision 1.0Feb 15, 2023Provider: repository / Type: Initial release

-
Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

-
Assembly

Deposited unit
A: ATP-dependent DNA helicase


Theoretical massNumber of molelcules
Total (without water)24,0031
Polymers24,0031
Non-polymers00
Water2,846158
1


  • Idetical with deposited unit
  • defined by author
  • Evidence: gel filtration
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)119.010, 120.670, 34.170
Angle α, β, γ (deg.)90.000, 90.000, 90.000
Int Tables number20
Space group name H-MC2221
Space group name HallC2c2
Symmetry operation#1: x,y,z
#2: x,-y,-z
#3: -x,y,-z+1/2
#4: -x,-y,z+1/2
#5: x+1/2,y+1/2,z
#6: x+1/2,-y+1/2,-z
#7: -x+1/2,y+1/2,-z+1/2
#8: -x+1/2,-y+1/2,z+1/2

-
Components

#1: Protein ATP-dependent DNA helicase


Mass: 24002.609 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Danio rerio (zebrafish) / Gene: LOC108180207 / Production host: Escherichia coli (E. coli) / References: UniProt: A0A2R8QJQ6, DNA helicase
#2: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 158 / Source method: isolated from a natural source / Formula: H2O
Has ligand of interestY

-
Experimental details

-
Experiment

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

-
Sample preparation

CrystalDensity Matthews: 2.56 Å3/Da / Density % sol: 51.87 %
Crystal growTemperature: 298 K / Method: vapor diffusion, sitting drop / pH: 8.5 / Details: 0.1 M Tris pH 8.5, 20% w/v PEG 6000

-
Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: PETRA III, EMBL c/o DESY / Beamline: P13 (MX1) / Wavelength: 0.9747 Å
DetectorType: DECTRIS PILATUS 6M / Detector: PIXEL / Date: Dec 4, 2020
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9747 Å / Relative weight: 1
ReflectionResolution: 1.9→100 Å / Num. obs: 37456 / % possible obs: 100 % / Redundancy: 10.6 % / Biso Wilson estimate: 23.32 Å2 / CC1/2: 0.998 / Rmerge(I) obs: 0.162 / Rrim(I) all: 0.172 / Net I/σ(I): 11.3
Reflection shellResolution: 1.9→1.95 Å / Redundancy: 5.3 % / Rmerge(I) obs: 1.02 / Mean I/σ(I) obs: 1.72 / Num. unique obs: 2724 / CC1/2: 0.621 / % possible all: 99.9

-
Processing

Software
NameVersionClassification
PHENIX1.20_4478refinement
PHENIX1.20_4478refinement
XDSdata reduction
XDSdata scaling
SHELXDEphasing
RefinementMethod to determine structure: SIR / Resolution: 1.9→42.37 Å / SU ML: 0.1445 / Cross valid method: FREE R-VALUE / σ(F): 1.35 / Phase error: 19.6658
Stereochemistry target values: GeoStd + Monomer Library + CDL v1.2
RfactorNum. reflection% reflection
Rfree0.2107 2783 7.43 %
Rwork0.162 34656 -
obs0.1655 37439 99.98 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.1 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso mean: 31.06 Å2
Refinement stepCycle: LAST / Resolution: 1.9→42.37 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms1666 0 0 158 1824
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00491705
X-RAY DIFFRACTIONf_angle_d0.84842302
X-RAY DIFFRACTIONf_chiral_restr0.0449257
X-RAY DIFFRACTIONf_plane_restr0.0063302
X-RAY DIFFRACTIONf_dihedral_angle_d6.5956231
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
1.9-1.930.3471380.27541695X-RAY DIFFRACTION99.84
1.93-1.970.23341400.2351722X-RAY DIFFRACTION100
1.97-2.010.251490.20421744X-RAY DIFFRACTION100
2.01-2.050.25441280.20171723X-RAY DIFFRACTION100
2.05-2.090.21731430.17371734X-RAY DIFFRACTION99.89
2.09-2.140.24181380.15841767X-RAY DIFFRACTION100
2.14-2.190.21931390.1561670X-RAY DIFFRACTION100
2.19-2.250.21051380.16451768X-RAY DIFFRACTION100
2.25-2.320.18831390.15451726X-RAY DIFFRACTION100
2.32-2.390.18011470.15861726X-RAY DIFFRACTION100
2.39-2.480.22211320.15221773X-RAY DIFFRACTION100
2.48-2.580.21321330.16271714X-RAY DIFFRACTION100
2.58-2.70.20551400.15941732X-RAY DIFFRACTION100
2.7-2.840.18831380.1671759X-RAY DIFFRACTION100
2.84-3.020.20621450.16121713X-RAY DIFFRACTION100
3.02-3.250.21041480.16121741X-RAY DIFFRACTION100
3.25-3.580.19051420.15041713X-RAY DIFFRACTION100
3.58-4.090.18041290.14371737X-RAY DIFFRACTION100
4.09-5.150.1821400.13121753X-RAY DIFFRACTION100
5.16-42.370.27861370.18331746X-RAY DIFFRACTION99.89
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)
10.533327544469-0.237877795855-0.0125560173010.356681099192-0.4743777949590.9603272337642.23052499265E-50.01416635291280.037201915930.109843926265-0.09842153570160.04588210469540.0921291420512-0.0961815769008-0.001131356055330.1639723360850.002620656385210.007244330346170.159570251912-0.01893917494770.18319074945436.019384528610.747549367428.6155650616
20.233282683514-0.02795750463860.03784760981250.158925562416-0.02524508354660.19202883679-0.0865520802440.265631011640.0865235186401-0.07267417742790.07502581372280.1622845076050.155968619394-0.298333499003-0.001123768661350.227643702708-0.005705230266780.008222619788250.246044873247-0.008247023927980.20044519454430.996470844419.945618055920.5906900643
30.002029945990250.01021290314340.004999229715120.05181361566340.02924822123640.04085812582290.1773225939920.4367441273570.245736377344-0.394042376297-0.170943830288-0.07245892358-0.2632500349590.439555666947-0.001906017976620.305141454777-0.00208075134099-0.001852100903150.362964426430.08429628633470.28089680648650.037910624733.745655925912.5424922859
40.8090816010380.321884134131-0.1024950787490.407986891556-0.5807911023571.0541916178-0.0175186900417-0.03277066507410.005292903927520.0414103880948-0.0508491638019-0.0492085855685-0.05410301062560.154981191427-3.26225875497E-50.1548026627440.00972922528077-0.02111351050970.181895824333-0.002118493722750.18263569644948.141480773121.882426199727.4189983799
50.1166422397760.1427478954530.04939105754180.3027942828250.2086132491210.173279507753-0.1124408248090.124842377874-0.0565811655908-0.01635725895390.001745172572720.1201606428240.109314264415-0.1160687664070.0001169845101680.2070292828130.02201205265570.0001577136559220.2144487773590.002612500966340.1913220312832.57094717725.554521086824.8598843406
Refinement TLS group

Refine-ID: X-RAY DIFFRACTION / Auth asym-ID: A / Label asym-ID: A

IDRefine TLS-IDSelection detailsAuth seq-IDLabel seq-ID
11chain 'A' and (resid 0 through 364 )0 - 3641 - 66
22chain 'A' and (resid 365 through 400 )365 - 40067 - 102
33chain 'A' and (resid 401 through 412 )401 - 412103 - 114
44chain 'A' and (resid 413 through 497 )413 - 497115 - 199
55chain 'A' and (resid 498 through 510 )498 - 510200 - 212

+
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