[English] 日本語
Yorodumi
- PDB-9ep3: Structure of the SA2/SCC1/WAPL complex -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 9ep3
TitleStructure of the SA2/SCC1/WAPL complex
Components
  • Cohesin subunit SA-2
  • Double-strand-break repair protein rad21 homolog
  • Wings apart-like protein homolog
KeywordsGENE REGULATION / Cohesin / Complex / HEAT Repeat / DNA binding / chromatin binding
Function / homology
Function and homology information


negative regulation of chromatin binding / ATP-dependent protein-DNA unloader activity / negative regulation of sister chromatid cohesion / negative regulation of mitotic metaphase/anaphase transition / Cohesin Loading onto Chromatin / meiotic cohesin complex / Establishment of Sister Chromatid Cohesion / establishment of meiotic sister chromatid cohesion / cohesin complex / mitotic cohesin complex ...negative regulation of chromatin binding / ATP-dependent protein-DNA unloader activity / negative regulation of sister chromatid cohesion / negative regulation of mitotic metaphase/anaphase transition / Cohesin Loading onto Chromatin / meiotic cohesin complex / Establishment of Sister Chromatid Cohesion / establishment of meiotic sister chromatid cohesion / cohesin complex / mitotic cohesin complex / positive regulation of sister chromatid cohesion / negative regulation of glial cell apoptotic process / negative regulation of G2/M transition of mitotic cell cycle / replication-born double-strand break repair via sister chromatid exchange / establishment of mitotic sister chromatid cohesion / chromatin looping / reciprocal meiotic recombination / sister chromatid cohesion / negative regulation of interleukin-1 beta production / mitotic spindle pole / lncRNA binding / negative regulation of DNA replication / mitotic sister chromatid segregation / positive regulation of interleukin-10 production / negative regulation of tumor necrosis factor production / chromosome, centromeric region / mitotic spindle assembly / SUMOylation of DNA damage response and repair proteins / intercellular bridge / cis-regulatory region sequence-specific DNA binding / protein localization to chromatin / Meiotic synapsis / Resolution of Sister Chromatid Cohesion / condensed nuclear chromosome / meiotic cell cycle / chromosome segregation / nuclear matrix / fibrillar center / Separation of Sister Chromatids / spindle pole / mitotic spindle / double-strand break repair / chromosome / midbody / DNA recombination / DNA-binding transcription factor binding / Estrogen-dependent gene expression / negative regulation of neuron apoptotic process / response to hypoxia / cell division / intracellular membrane-bounded organelle / apoptotic process / chromatin binding / regulation of transcription by RNA polymerase II / chromatin / nucleolus / nucleoplasm / nucleus / membrane / cytosol / cytoplasm
Similarity search - Function
WAPL domain / Wings apart-like protein, C-terminal / Wings apart-like protein / Wings apart-like protein regulation of heterochromatin / WAPL domain profile. / : / Cohesin subunit SCC3/SA, HEAT-repeats domain / STAG / Stromalin conservative domain / Cohesin subunit Scc3/SA ...WAPL domain / Wings apart-like protein, C-terminal / Wings apart-like protein / Wings apart-like protein regulation of heterochromatin / WAPL domain profile. / : / Cohesin subunit SCC3/SA, HEAT-repeats domain / STAG / Stromalin conservative domain / Cohesin subunit Scc3/SA / STAG domain / Stromalin conservative domain / Stromalin conservative (SCD) domain profile. / : / Rad21/Rec8-like protein, C-terminal, eukaryotic / Rad21/Rec8-like protein, N-terminal / Rad21/Rec8-like protein / Conserved region of Rad21 / Rec8 like protein / N terminus of Rad21 / Rec8 like protein / ScpA-like, C-terminal / Armadillo-like helical / Armadillo-type fold / Winged helix DNA-binding domain superfamily
Similarity search - Domain/homology
Double-strand-break repair protein rad21 homolog / Wings apart-like protein homolog / Cohesin subunit SA-2
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3.08 Å
AuthorsGraham, J.J. / Panne, D.
Funding support United Kingdom, 2items
OrganizationGrant numberCountry
Wellcome Trust221881/Z/20/Z United Kingdom
Medical Research Council (MRC, United Kingdom)MR/W001667/1 United Kingdom
CitationJournal: To Be Published
Title: Structural basis for cohesin release and control of genome looping by WAPL
Authors: Graham, J.J. / Panne, D.
History
DepositionMar 16, 2024Deposition site: PDBE / Processing site: PDBE
Revision 1.0Oct 1, 2025Provider: repository / Type: Initial release

-
Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

-
Assembly

Deposited unit
A: Cohesin subunit SA-2
B: Double-strand-break repair protein rad21 homolog
C: Wings apart-like protein homolog


Theoretical massNumber of molelcules
Total (without water)132,3023
Polymers132,3023
Non-polymers00
Water1,06359
1


  • Idetical with deposited unit
  • defined by author&software
  • Evidence: gel filtration
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area8440 Å2
ΔGint-44 kcal/mol
Surface area47840 Å2
MethodPISA
Unit cell
Length a, b, c (Å)78.433, 107.440, 181.913
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number19
Space group name H-MP212121

-
Components

#1: Protein Cohesin subunit SA-2 / SCC3 homolog 2 / Stromal antigen 2


Mass: 113610.039 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: STAG2, SA2 / Production host: Escherichia coli (E. coli) / References: UniProt: Q8N3U4
#2: Protein Double-strand-break repair protein rad21 homolog / 64-kDa carboxy-terminal product / 65-kDa carboxy-terminal product


Mass: 16049.612 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: RAD21, HR21, KIAA0078, NXP1, SCC1 / Production host: Escherichia coli (E. coli) / References: UniProt: O60216
#3: Protein/peptide Wings apart-like protein homolog / Friend of EBNA2 protein / WAPL cohesin release factor


Mass: 2641.894 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) Homo sapiens (human) / References: UniProt: Q7Z5K2
#4: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 59 / Source method: isolated from a natural source / Formula: H2O
Has protein modificationN

-
Experimental details

-
Experiment

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

-
Sample preparation

CrystalDensity Matthews: 2.9 Å3/Da / Density % sol: 57.54 %
Crystal growTemperature: 291 K / Method: vapor diffusion, hanging drop
Details: 0.06M Morpheus Divalents mix, 0.1M Morpheus buffer system 1, 48% (v/v) Morpheus EOD_P8K

-
Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: ESRF / Beamline: MASSIF-1 / Wavelength: 0.9655 Å
DetectorType: DECTRIS PILATUS3 2M / Detector: PIXEL / Date: Oct 1, 2021
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9655 Å / Relative weight: 1
ReflectionResolution: 3.08→47.97 Å / Num. obs: 28667 / % possible obs: 98.6 % / Redundancy: 4.4 % / CC1/2: 0.99 / Net I/σ(I): 9.2
Reflection shellResolution: 3.08→3.26 Å / Num. unique obs: 2797 / CC1/2: 0.375 / % possible all: 97.4

-
Processing

Software
NameVersionClassification
PHENIX(1.19.2_4158: ???)refinement
XDSdata reduction
XDSdata scaling
PHENIXphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT / Resolution: 3.08→47.97 Å / SU ML: 0.51 / Cross valid method: FREE R-VALUE / σ(F): 1.34 / Phase error: 30.54 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2682 1391 4.85 %
Rwork0.2244 --
obs0.2265 28667 97.86 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Refinement stepCycle: LAST / Resolution: 3.08→47.97 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms8314 0 0 60 8374
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0038473
X-RAY DIFFRACTIONf_angle_d0.52211427
X-RAY DIFFRACTIONf_dihedral_angle_d4.3361104
X-RAY DIFFRACTIONf_chiral_restr0.0331295
X-RAY DIFFRACTIONf_plane_restr0.0031447
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
3.08-3.190.41841290.39382594X-RAY DIFFRACTION95
3.19-3.310.36721330.31972726X-RAY DIFFRACTION99
3.31-3.460.27391310.28512707X-RAY DIFFRACTION98
3.46-3.650.39291370.28052705X-RAY DIFFRACTION99
3.65-3.870.26361470.22042728X-RAY DIFFRACTION99
3.88-4.170.25541290.21052746X-RAY DIFFRACTION99
4.17-4.590.25361320.19642766X-RAY DIFFRACTION99
4.59-5.260.22731700.20212709X-RAY DIFFRACTION98
5.26-6.620.30161520.24932794X-RAY DIFFRACTION99
6.62-47.970.23321310.19092801X-RAY DIFFRACTION94
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)
14.22541.46673.28732.61580.25226.60420.42480.2632-0.5601-0.0950.1831-0.5280.00080.71870.60921.332-0.059-0.36371.3556-0.46880.589-45.2292-40.9287-23.4529
25.67841.1388-2.4233.8036-1.06013.3211-0.51571.0336-1.1238-0.53530.0979-0.66690.6274-0.05640.15370.7494-0.0414-0.03510.6511-0.06990.705-42.8883-42.4471-13.1391
32.16760.5772-1.40041.66190.67152.1460.4559-0.3341-0.74550.3828-0.4850.539-0.3337-0.93170.33340.67020.05080.05940.41650.11750.6947-51.8717-36.40654.8284
47.46773.8494-1.34765.6365-0.60810.18190.305-0.5567-0.62930.7306-0.2661-0.0045-0.0366-0.24170.02160.67190.01670.03520.38860.05360.5556-42.8149-27.27973.7109
52.99193.31361.59428.29145.5215.5056-0.85480.58360.46631.127-0.18012.55930.04322.23460.75951.2746-0.06620.53531.46320.06212.1472-52.5846-13.75848.1882
63.3813-1.15752.55334.0432-3.79496.938-0.1718-0.44930.18620.2129-0.135-0.3955-0.4673-0.26960.21210.72950.08730.1210.54290.01010.7011-40.5761-2.67221.1304
75.84950.9976-0.39781.69280.64756.84830.0260.5295-0.2960.4599-0.03110.00960.5209-0.38670.5430.75090.19720.22620.44360.17410.2579-50.794210.9222-1.5304
89.76540.7393-0.54891.59820.72948.08180.1538-0.35-0.00810.22190.2027-0.2501-0.2754-0.9188-0.20951.07060.15170.10820.56750.17080.9138-49.872215.3907-8.9856
97.0523-0.54451.43742.54550.42927.9795-0.15440.0868-0.0537-0.4602-0.37841.3808-0.81880.01050.18550.96280.2580.09140.65240.25610.849-51.030215.7782-15.6019
105.27120.4165-1.69973.5264-1.63734.88610.37120.63420.5238-0.17680.19060.8138-0.2078-0.8787-0.2530.91920.27420.08160.84580.31211.0663-53.2330.983-23.6074
111.42351.36830.79353.6578-0.48364.42740.86440.36661.65070.90610.06152.6407-0.82990.036-0.43061.41580.14550.64880.69340.20791.6111-38.54348.5482-32.0401
126.47490.635-0.23262.81741.58144.17560.09510.72320.4792-0.01570.55150.0657-0.7060.1495-0.52011.2810.03060.30310.87010.29071.1316-31.828740.4494-34.9558
132.3953-1.5888-3.60576.1059-2.00229.23790.07221.47091.0858-1.595-0.9743-1.14480.73470.46110.78041.56050.12630.44311.34670.2561.131-24.504136.005-45.1503
144.5523-0.61381.36823.45972.0375.1721-0.24611.35761.3196-0.5119-0.09870.0366-0.75340.6673-0.15071.21130.04590.38141.2574-0.05520.9066-23.876226.1077-43.548
155.50291.571-6.61495.5370.32848.9255-0.2737-0.37540.33520.1790.8775-1.3116-0.88730.0754-0.8071.29160.4938-0.11681.4882-0.19250.801-14.086720.1874-24.1208
163.089-0.66910.84313.89250.48322.2715-0.0346-0.56680.72660.3078-0.68811.0279-2.692-1.3252-0.13092.09850.69770.18021.2394-0.07950.791-22.8819.4222-20.2214
175.6046-3.74541.67348.90551.73834.0633-0.21580.558-0.1947-0.32710.511-0.71980.17290.613-0.30530.9970.08870.18950.9981-0.20840.6639-14.536810.1614-36.8523
187.10280.1355-0.71073.4354-2.88146.44910.63840.0438-0.0170.18180.0923-0.13731.4753-0.7001-0.72411.22430.02150.31681.4324-0.27511.1101-2.94130.7192-38.0962
199.0811-6.1709-5.33755.15494.10853.7745-1.6510.8585-0.47520.90531.3488-1.94321.76930.60120.40771.2397-0.05990.29711.3367-0.39151.635715.58914.0329-40.366
204.67550.9709-1.00899.72973.24855.1361-0.0996-0.5512-1.1364-0.6774-0.0786-0.5831-0.27631.09650.57171.45870.31290.24671.2646-0.12731.45234.8809-7.4878-43.2811
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1(chain A and resid 80:90)
2X-RAY DIFFRACTION2(chain A and resid 91:200)
3X-RAY DIFFRACTION3(chain A and resid 201:264)
4X-RAY DIFFRACTION4(chain A and resid 265:355)
5X-RAY DIFFRACTION5(chain A and resid 356:363)
6X-RAY DIFFRACTION6(chain A and resid 364:423)
7X-RAY DIFFRACTION7(chain A and resid 424:468)
8X-RAY DIFFRACTION8(chain A and resid 469:502)
9X-RAY DIFFRACTION9(chain A and resid 503:557)
10X-RAY DIFFRACTION10(chain A and resid 558:651)
11X-RAY DIFFRACTION11(chain A and resid 652:675)
12X-RAY DIFFRACTION12(chain A and resid 676:755)
13X-RAY DIFFRACTION13(chain A and resid 756:777)
14X-RAY DIFFRACTION14(chain A and resid 778:823)
15X-RAY DIFFRACTION15(chain A and resid 824:852)
16X-RAY DIFFRACTION16(chain A and resid 853:861)
17X-RAY DIFFRACTION17(chain A and resid 862:930)
18X-RAY DIFFRACTION18(chain A and resid 931:984)
19X-RAY DIFFRACTION19(chain A and resid 985:998)
20X-RAY DIFFRACTION20(chain A and resid 999:1048)

+
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