[English] 日本語
Yorodumi
- PDB-7vou: The crystal structure of human forkhead box protein in complex wi... -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 7vou
TitleThe crystal structure of human forkhead box protein in complex with DNA 1
Components
  • DNA (5'-D(*AP*CP*TP*TP*GP*TP*TP*TP*AP*CP*AP*TP*TP*TP*TP*G)-3')
  • DNA (5'-D(*CP*AP*AP*AP*AP*TP*GP*TP*AP*AP*AP*CP*AP*AP*GP*T)-3')
  • Forkhead box protein L2
KeywordsTRANSCRIPTION/DNA / DNA-protein complex / transcription factor / TRANSCRIPTION / TRANSCRIPTION-DNA complex
Function / homology
Function and homology information


granulosa cell differentiation / female somatic sex determination / extraocular skeletal muscle development / cysteine-type endopeptidase regulator activity involved in apoptotic process / oocyte growth / positive regulation of luteinizing hormone secretion / embryonic eye morphogenesis / positive regulation of follicle-stimulating hormone secretion / apoptotic DNA fragmentation / Flemming body ...granulosa cell differentiation / female somatic sex determination / extraocular skeletal muscle development / cysteine-type endopeptidase regulator activity involved in apoptotic process / oocyte growth / positive regulation of luteinizing hormone secretion / embryonic eye morphogenesis / positive regulation of follicle-stimulating hormone secretion / apoptotic DNA fragmentation / Flemming body / ubiquitin conjugating enzyme binding / uterus development / positive regulation of cysteine-type endopeptidase activity involved in apoptotic process / SUMOylation of transcription factors / single fertilization / anatomical structure morphogenesis / ovarian follicle development / nuclear estrogen receptor binding / sequence-specific double-stranded DNA binding / DNA-binding transcription activator activity, RNA polymerase II-specific / cell differentiation / DNA-binding transcription factor activity, RNA polymerase II-specific / positive regulation of apoptotic process / RNA polymerase II cis-regulatory region sequence-specific DNA binding / DNA-binding transcription factor activity / negative regulation of DNA-templated transcription / chromatin / regulation of transcription by RNA polymerase II / positive regulation of DNA-templated transcription / negative regulation of transcription by RNA polymerase II / DNA binding / nucleoplasm / nucleus
Similarity search - Function
Fork head domain conserved site1 / Fork head domain signature 1. / Fork head domain / Forkhead domain / Fork head domain profile. / FORKHEAD / Fork head domain conserved site 2 / Fork head domain signature 2. / Winged helix DNA-binding domain superfamily / Winged helix-like DNA-binding domain superfamily
Similarity search - Domain/homology
DNA / DNA (> 10) / Forkhead box protein L2
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3.1 Å
AuthorsChoi, Y. / Yoon, H.J. / Lee, H.H.
Funding support Korea, Republic Of, 1items
OrganizationGrant numberCountry
National Research Foundation (NRF, Korea)2018R1A2B2008142 Korea, Republic Of
CitationJournal: Nucleic Acids Res. / Year: 2022
Title: FOXL2 and FOXA1 cooperatively assemble on the TP53 promoter in alternative dimer configurations.
Authors: Choi, Y. / Luo, Y. / Lee, S. / Jin, H. / Yoon, H.J. / Hahn, Y. / Bae, J. / Lee, H.H.
History
DepositionOct 14, 2021Deposition site: PDBJ / Processing site: PDBJ
Revision 1.0Aug 17, 2022Provider: repository / Type: Initial release
Revision 1.1Aug 24, 2022Group: Database references / Category: citation / Item: _citation.pdbx_database_id_PubMed / _citation.title
Revision 1.2Sep 7, 2022Group: Database references / Category: citation
Item: _citation.journal_volume / _citation.page_first / _citation.page_last
Revision 1.3Nov 29, 2023Group: Data collection / Refinement description
Category: chem_comp_atom / chem_comp_bond / pdbx_initial_refinement_model

-
Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

-
Assembly

Deposited unit
A: DNA (5'-D(*AP*CP*TP*TP*GP*TP*TP*TP*AP*CP*AP*TP*TP*TP*TP*G)-3')
B: DNA (5'-D(*CP*AP*AP*AP*AP*TP*GP*TP*AP*AP*AP*CP*AP*AP*GP*T)-3')
C: Forkhead box protein L2


Theoretical massNumber of molelcules
Total (without water)22,6433
Polymers22,6433
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author&software
  • Evidence: isothermal titration calorimetry
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area2960 Å2
ΔGint-21 kcal/mol
Surface area10380 Å2
MethodPISA
Unit cell
Length a, b, c (Å)47.987, 47.987, 164.414
Angle α, β, γ (deg.)90.000, 90.000, 90.000
Int Tables number92
Space group name H-MP41212

-
Components

#1: DNA chain DNA (5'-D(*AP*CP*TP*TP*GP*TP*TP*TP*AP*CP*AP*TP*TP*TP*TP*G)-3')


Mass: 4869.173 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) Homo sapiens (human)
#2: DNA chain DNA (5'-D(*CP*AP*AP*AP*AP*TP*GP*TP*AP*AP*AP*CP*AP*AP*GP*T)-3')


Mass: 4923.258 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) Homo sapiens (human)
#3: Protein Forkhead box protein L2


Mass: 12850.727 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: FOXL2 / Production host: Escherichia coli (E. coli) / References: UniProt: P58012

-
Experimental details

-
Experiment

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

-
Sample preparation

CrystalDensity Matthews: 2.09 Å3/Da / Density % sol: 41.16 %
Crystal growTemperature: 291 K / Method: vapor diffusion, hanging drop
Details: 0.1 M Bis-tris pH 5.5, 0.15 M NaCl, and 26% PEG 3350

-
Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: PAL/PLS / Beamline: 5C (4A) / Wavelength: 1 Å
DetectorType: DECTRIS EIGER X 9M / Detector: PIXEL / Date: Nov 19, 2019
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 3.1→50 Å / Num. obs: 3950 / % possible obs: 100 % / Redundancy: 21.1 % / Biso Wilson estimate: 84.45 Å2 / Rmerge(I) obs: 0.091 / Rpim(I) all: 0.02 / Rrim(I) all: 0.093 / Χ2: 0.973 / Net I/σ(I): 9.8 / Num. measured all: 83510
Reflection shell

Diffraction-ID: 1

Resolution (Å)Redundancy (%)Rmerge(I) obsNum. unique obsCC1/2Rpim(I) allRrim(I) allΧ2% possible all
3.1-3.1519.50.8581850.9880.1920.880.671100
3.15-3.2119.30.4781910.9970.1110.4910.693100
3.21-3.27200.5581810.990.1260.5720.683100
3.27-3.3418.40.3171920.9950.0750.3260.746100
3.34-3.4118.60.2461910.9960.0580.2530.735100
3.41-3.4920.20.361860.9830.0810.370.751100
3.49-3.58210.2761910.9920.0610.2830.729100
3.58-3.6822.30.2551950.990.0530.260.759100
3.68-3.7821.40.2491890.990.0530.2541.132100
3.78-3.91220.1921860.9930.0410.1961.029100
3.91-4.0423.20.1371960.9960.0280.140.835100
4.04-4.2123.70.11950.9980.0210.1020.864100
4.21-4.423.10.0991930.9950.0210.1010.841100
4.4-4.6321.90.1231900.9960.0260.1262.854100
4.63-4.92210.0722080.9980.0160.0740.989100
4.92-5.323.60.0652030.9990.0130.0660.865100
5.3-5.8322.40.0591970.9990.0120.060.816100
5.83-6.6719.50.0522110.9990.0120.0540.999100
6.67-8.421.90.0462150.9990.010.0470.888100
8.4-50200.0452550.9980.010.0461.36599.6

-
Processing

Software
NameVersionClassification
PHENIX1.19.1_4122refinement
HKL-2000data scaling
PDB_EXTRACT3.27data extraction
DENZOdata reduction
MOLREPphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 7CBY
Resolution: 3.1→46.07 Å / SU ML: 0.32 / Cross valid method: THROUGHOUT / σ(F): 1.33 / Phase error: 25.89 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2802 384 9.97 %
Rwork0.221 3468 -
obs0.2269 3852 98.69 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso max: 185.62 Å2 / Biso mean: 90.479 Å2 / Biso min: 36.57 Å2
Refinement stepCycle: final / Resolution: 3.1→46.07 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms706 650 0 0 1356
Num. residues----118
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Rfactor Rfree error: 0 / Total num. of bins used: 3

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkNum. reflection all% reflection obs (%)
3.1-3.550.28631190.25351088120797
3.55-4.470.27791280.23051144127299
4.47-46.070.27961370.20751236137399
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)
17.10540.317-0.42422.294-3.54075.2418-0.2104-0.31460.40220.42350.0473-0.62280.14570.0754-0.11890.51120.0219-0.05850.514-0.04820.5657-0.5944-25.00917.009
24.55450.5250.07182.5063-0.16184.55520.2471-0.4872-0.0545-0.391-0.1049-1.31250.37580.5304-0.0490.510.0505-0.00110.48410.03170.65361.5934-23.76817.5897
38.34741.74381.02884.6109-0.06868.6068-0.17611.06010.5403-0.51080.3364-0.45850.3475-0.1716-0.16120.61370.01460.06340.48980.16160.3995-4.8393-19.42123.3715
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1(chain 'A' and resid 1 through 16)A1 - 16
2X-RAY DIFFRACTION2(chain 'B' and resid 1 through 16)B1 - 16
3X-RAY DIFFRACTION3(chain 'C' and resid 181 through 266)C181 - 266

+
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