[English] 日本語
Yorodumi
- PDB-7bv7: INTS3 complexed with INTS6 -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 7bv7
TitleINTS3 complexed with INTS6
Components
  • Integrator complex subunit 3
  • Integrator complex subunit 6
KeywordsRECOMBINATION / DNA double strand break repair INTS3 INTS6 SSB1
Function / homology
Function and homology information


SOSS complex / snRNA 3'-end processing / snRNA processing / integrator complex / regulation of transcription elongation by RNA polymerase II / mitotic G2/M transition checkpoint / response to ionizing radiation / RNA polymerase II transcribes snRNA genes / double-strand break repair via homologous recombination / transmembrane signaling receptor activity ...SOSS complex / snRNA 3'-end processing / snRNA processing / integrator complex / regulation of transcription elongation by RNA polymerase II / mitotic G2/M transition checkpoint / response to ionizing radiation / RNA polymerase II transcribes snRNA genes / double-strand break repair via homologous recombination / transmembrane signaling receptor activity / actin cytoskeleton / site of double-strand break / DNA repair / DNA damage response / nucleoplasm / nucleus / cytoplasm
Similarity search - Function
Integrator complex subunit 3, N-terminal / Integrator complex subunit 3 / Integrator complex subunit 3 N-terminal / INTS6/SAGE1/DDX26B/CT45, C-terminal / INTS6/SAGE1/DDX26B/CT45 C-terminus / von Willebrand factor type A domain / VWFA domain profile. / von Willebrand factor, type A / von Willebrand factor A-like domain superfamily
Similarity search - Domain/homology
Integrator complex subunit 3 / Integrator complex subunit 6
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.4 Å
AuthorsJia, Y. / Bharath, S.R. / Song, H.
CitationJournal: Cell Discov / Year: 2021
Title: Crystal structure of the INTS3/INTS6 complex reveals the functional importance of INTS3 dimerization in DSB repair.
Authors: Jia, Y. / Cheng, Z. / Bharath, S.R. / Sun, Q. / Su, N. / Huang, J. / Song, H.
History
DepositionApr 9, 2020Deposition site: PDBJ / Processing site: PDBJ
Revision 1.0Jul 14, 2021Provider: repository / Type: Initial release
Revision 1.1Jul 27, 2022Group: Database references / Category: citation / citation_author / database_2
Item: _citation.country / _citation.journal_abbrev ..._citation.country / _citation.journal_abbrev / _citation.journal_id_CSD / _citation.journal_id_ISSN / _citation.journal_volume / _citation.page_first / _citation.page_last / _citation.pdbx_database_id_DOI / _citation.pdbx_database_id_PubMed / _citation.title / _citation.year / _citation_author.identifier_ORCID / _database_2.pdbx_DOI / _database_2.pdbx_database_accession
Revision 1.2May 29, 2024Group: Data collection / Category: chem_comp_atom / chem_comp_bond

-
Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

-
Assembly

Deposited unit
A: Integrator complex subunit 3
B: Integrator complex subunit 3
C: Integrator complex subunit 6


Theoretical massNumber of molelcules
Total (without water)111,2443
Polymers111,2443
Non-polymers00
Water3,261181
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)60.570, 126.030, 84.440
Angle α, β, γ (deg.)90.000, 102.120, 90.000
Int Tables number4
Space group name H-MP1211

-
Components

#1: Protein Integrator complex subunit 3 / Int3 / SOSS complex subunit A / Sensor of single-strand DNA complex subunit A / Sensor of ssDNA subunit A


Mass: 50291.566 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: INTS3, C1orf193, C1orf60 / Production host: Escherichia coli (E. coli) / References: UniProt: Q68E01
#2: Protein Integrator complex subunit 6 / Int6 / DBI-1 / Protein DDX26 / Protein deleted in cancer 1 / DICE1


Mass: 10660.439 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: INTS6, DBI1, DDX26, DDX26A / Production host: Escherichia coli (E. coli) / References: UniProt: Q9UL03
#3: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 181 / 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: 2.83 Å3/Da / Density % sol: 56.58 %
Crystal growTemperature: 288 K / Method: vapor diffusion, hanging drop
Details: 1.7 M Ammonium citrate pH 7.0 4% pentaerythritol ethoxylate

-
Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: Australian Synchrotron / Beamline: MX2 / Wavelength: 1 Å
DetectorType: DECTRIS EIGER X 16M / Detector: PIXEL / Date: Aug 3, 2018
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 2.4→49.45 Å / Num. obs: 43480 / % possible obs: 90 % / Redundancy: 2.7 % / CC1/2: 0.995 / Rmerge(I) obs: 0.08 / Net I/σ(I): 4.9
Reflection shellResolution: 2.4→2.49 Å / Rmerge(I) obs: 0.75 / Num. unique obs: 4704 / CC1/2: 0.53

-
Processing

Software
NameVersionClassification
PHENIX1.17.1_3660refinement
PDB_EXTRACT3.25data extraction
XDSdata reduction
Aimlessdata scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT / Resolution: 2.4→43.95 Å / SU ML: 0.29 / Cross valid method: THROUGHOUT / σ(F): 1.36 / Phase error: 25.31
RfactorNum. reflection% reflection
Rfree0.2492 2124 4.89 %
Rwork0.2048 --
obs0.2069 43428 89.68 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å
Displacement parametersBiso max: 131.09 Å2 / Biso mean: 53.5158 Å2 / Biso min: 15.42 Å2
Refinement stepCycle: final / Resolution: 2.4→43.95 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms6001 0 0 181 6182
Biso mean---48.15 -
Num. residues----758
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Rfactor Rfree error: 0 / Total num. of bins used: 15

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkNum. reflection all% reflection obs (%)
2.4-2.460.30541340.25162850298493
2.46-2.520.28491670.24352782294992
2.52-2.590.29361220.24022841296392
2.59-2.660.27641540.23432819297392
2.66-2.750.31811490.23352779292891
2.75-2.850.25091340.21832809294392
2.85-2.960.26741280.20622781290991
2.96-3.090.28071550.20522795295091
3.09-3.260.23251400.20232747288790
3.26-3.460.22661490.1912720286989
3.46-3.730.23691450.18172709285488
3.73-4.10.23721530.17392676282988
4.1-4.70.20891340.17272640277485
4.7-5.910.2271380.20872664280287
5.92-43.950.26971220.23212692281485
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)
13.03380.5796-0.09521.97360.24062.0619-0.0487-0.060.62150.003-0.16350.8037-0.2712-0.48620.04870.22140.0601-0.04970.2789-0.09790.5463-24.262164.922222.5114
22.32280.4019-0.54524.29550.86531.0255-0.2515-0.0724-0.81890.6384-0.0719-0.10070.5696-0.06870.18440.74310.01330.16860.2709-0.02920.5444-2.222825.318117.099
30.5145-0.3877-0.55991.49570.18411.03710.26261.22380.0994-0.7716-0.5406-0.20190.25510.3820.20920.8180.30350.13681.50830.05130.553628.359149.9807-10.7069
43.0015-0.8887-1.06821.0055-0.77822.5750.16490.47840.0583-0.0817-0.2513-0.29620.12790.87730.02810.25320.04450.0050.6129-0.02320.257619.962450.91047.4283
51.5708-0.576-0.92772.01491.44553.8709-0.2941-0.3502-0.07330.68910.160.23770.40490.09520.11010.39220.0650.00290.2756-0.00030.2397-1.429657.660540.4465
62.6579-0.70510.32984.6553-1.40853.9508-0.00830.38420.2735-0.274-0.04670.27120.3141-0.2494-0.0070.3753-0.0454-0.03260.32940.07660.3575-7.700166.77495.4462
71.7672-0.2194-0.20932.4799-0.77984.09320.29760.37490.3529-0.1436-0.05480.5162-0.2502-0.7203-0.23410.3646-0.0023-0.04640.30820.10540.365-6.325774.99925.0367
82.3339-1.98731.19635.679-6.12137.58380.15880.46770.56590.4154-0.8063-1.6328-1.25250.80220.61160.5712-0.01760.02070.40840.10050.59011.579782.0644.4386
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1chain 'A' and (resid 595 through 850 )A595 - 850
2X-RAY DIFFRACTION2chain 'A' and (resid 851 through 972 )A851 - 972
3X-RAY DIFFRACTION3chain 'B' and (resid 583 through 667 )B583 - 667
4X-RAY DIFFRACTION4chain 'B' and (resid 668 through 781 )B668 - 781
5X-RAY DIFFRACTION5chain 'B' and (resid 782 through 972 )B782 - 972
6X-RAY DIFFRACTION6chain 'C' and (resid 808 through 827 )C808 - 827
7X-RAY DIFFRACTION7chain 'C' and (resid 828 through 860 )C828 - 860
8X-RAY DIFFRACTION8chain 'C' and (resid 861 through 881 )C861 - 881

+
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