[English] 日本語
Yorodumi
- PDB-8wzl: Arabidopsis thaliana Histone deacetylase 7 (HDA7) -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 8wzl
TitleArabidopsis thaliana Histone deacetylase 7 (HDA7)
ComponentsHistone deacetylase 7
KeywordsGENE REGULATION / Histone Deacetylase
Function / homology
Function and homology information


embryo sac development / seed germination / embryo development ending in seed dormancy / histone deacetylase / histone deacetylase activity / zinc ion binding / nucleus
Similarity search - Function
Histone deacetylase / : / Histone deacetylase family / Histone deacetylase domain / Histone deacetylase domain superfamily / Histone deacetylase domain / Ureohydrolase domain superfamily
Similarity search - Domain/homology
Histone deacetylase 7
Similarity search - Component
Biological speciesArabidopsis thaliana (thale cress)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.5 Å
AuthorsSaharan, K. / Vasudevan, D.
Funding support India, 2items
OrganizationGrant numberCountry
Department of Biotechnology (DBT, India)BT/INF/22/SP22660/2017 India
Department of Biotechnology (DBT, India)BT/INF/22/SP33046/2019 India
CitationJournal: Curr Res Struct Biol / Year: 2024
Title: Structure-function analyses reveal Arabidopsis thaliana HDA7 to be an inactive histone deacetylase.
Authors: Saharan, K. / Baral, S. / Shaikh, N.H. / Vasudevan, D.
History
DepositionNov 2, 2023Deposition site: PDBJ / Processing site: PDBJ
Revision 1.0May 29, 2024Provider: repository / Type: Initial release
Revision 1.1Mar 26, 2025Group: Data collection / Structure summary / Category: diffrn_source / pdbx_entry_details
Item: _diffrn_source.pdbx_synchrotron_beamline / _diffrn_source.type / _pdbx_entry_details.has_protein_modification

-
Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

-
Assembly

Deposited unit
A: Histone deacetylase 7
hetero molecules


Theoretical massNumber of molelcules
Total (without water)43,8764
Polymers43,5881
Non-polymers2883
Water3,315184
1


  • Idetical with deposited unit
  • defined by author&software
  • Evidence: SAXS
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area160 Å2
ΔGint-10 kcal/mol
Surface area15260 Å2
MethodPISA
Unit cell
Length a, b, c (Å)47.308, 74.475, 47.590
Angle α, β, γ (deg.)90.00, 112.02, 90.00
Int Tables number4
Space group name H-MP1211

-
Components

#1: Protein Histone deacetylase 7


Mass: 43588.203 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Arabidopsis thaliana (thale cress) / Gene: HDA7, At5g35600, K2K18.5 / Production host: Escherichia coli BL21(DE3) (bacteria) / References: UniProt: Q9FH09, histone deacetylase
#2: Chemical ChemComp-SO4 / SULFATE ION


Mass: 96.063 Da / Num. of mol.: 3 / Source method: isolated from a natural source / Formula: SO4
#3: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 184 / Source method: isolated from a natural source / Formula: H2O
Has ligand of interestN
Has protein modificationN

-
Experimental details

-
Experiment

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

-
Sample preparation

CrystalDensity Matthews: 1.83 Å3/Da / Density % sol: 32.74 %
Crystal growTemperature: 291.15 K / Method: vapor diffusion, hanging drop / pH: 7.5 / Details: 0.1M HEPES, 25% PEG 3350

-
Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: ESRF / Beamline: ID23-2 / Wavelength: 0.9794 Å
DetectorType: DECTRIS PILATUS3 2M / Detector: PIXEL / Date: Feb 19, 2021
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9794 Å / Relative weight: 1
ReflectionResolution: 1.5→43.9 Å / Num. obs: 47979 / % possible obs: 98.1 % / Redundancy: 7.2 % / CC1/2: 0.93 / Net I/σ(I): 9.7
Reflection shellResolution: 1.5→1.53 Å / Redundancy: 7.9 % / Mean I/σ(I) obs: 3.2 / Num. unique obs: 2387 / CC1/2: 0.703 / % possible all: 96.8

-
Processing

Software
NameVersionClassification
REFMAC5.8.0415refinement
DIALSdata reduction
Aimlessdata scaling
PHENIXphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT / Resolution: 1.5→43.9 Å / Cor.coef. Fo:Fc: 0.964 / Cor.coef. Fo:Fc free: 0.952 / SU B: 3.368 / SU ML: 0.056 / Cross valid method: THROUGHOUT / ESU R: 0.105 / ESU R Free: 0.081 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
RfactorNum. reflection% reflectionSelection details
Rfree0.19929 2458 5.1 %RANDOM
Rwork0.15715 ---
obs0.15922 45496 97.9 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK
Displacement parametersBiso mean: 14.675 Å2
Baniso -1Baniso -2Baniso -3
1-1.69 Å20 Å20.46 Å2
2---1.34 Å2-0 Å2
3----0.54 Å2
Refinement stepCycle: 1 / Resolution: 1.5→43.9 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms2961 0 15 184 3160
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0080.0123069
X-RAY DIFFRACTIONr_bond_other_d0.0010.0162790
X-RAY DIFFRACTIONr_angle_refined_deg1.5421.6634179
X-RAY DIFFRACTIONr_angle_other_deg0.551.5786415
X-RAY DIFFRACTIONr_dihedral_angle_1_deg6.2965379
X-RAY DIFFRACTIONr_dihedral_angle_2_deg8.691518
X-RAY DIFFRACTIONr_dihedral_angle_3_deg13.37710475
X-RAY DIFFRACTIONr_dihedral_angle_4_deg
X-RAY DIFFRACTIONr_chiral_restr0.0880.2452
X-RAY DIFFRACTIONr_gen_planes_refined0.0090.023642
X-RAY DIFFRACTIONr_gen_planes_other0.0010.02724
X-RAY DIFFRACTIONr_nbd_refined
X-RAY DIFFRACTIONr_nbd_other
X-RAY DIFFRACTIONr_nbtor_refined
X-RAY DIFFRACTIONr_nbtor_other
X-RAY DIFFRACTIONr_xyhbond_nbd_refined
X-RAY DIFFRACTIONr_xyhbond_nbd_other
X-RAY DIFFRACTIONr_metal_ion_refined
X-RAY DIFFRACTIONr_metal_ion_other
X-RAY DIFFRACTIONr_symmetry_vdw_refined
X-RAY DIFFRACTIONr_symmetry_vdw_other
X-RAY DIFFRACTIONr_symmetry_hbond_refined
X-RAY DIFFRACTIONr_symmetry_hbond_other
X-RAY DIFFRACTIONr_symmetry_metal_ion_refined
X-RAY DIFFRACTIONr_symmetry_metal_ion_other
X-RAY DIFFRACTIONr_mcbond_it0.9191.4311507
X-RAY DIFFRACTIONr_mcbond_other0.9191.4311507
X-RAY DIFFRACTIONr_mcangle_it1.3372.5811883
X-RAY DIFFRACTIONr_mcangle_other1.3372.5821884
X-RAY DIFFRACTIONr_scbond_it1.0151.6661562
X-RAY DIFFRACTIONr_scbond_other1.0091.6511551
X-RAY DIFFRACTIONr_scangle_it
X-RAY DIFFRACTIONr_scangle_other1.4082.9492277
X-RAY DIFFRACTIONr_long_range_B_refined2.12416.463458
X-RAY DIFFRACTIONr_long_range_B_other2.05415.473426
X-RAY DIFFRACTIONr_rigid_bond_restr3.16435859
X-RAY DIFFRACTIONr_sphericity_free
X-RAY DIFFRACTIONr_sphericity_bonded
LS refinement shellResolution: 1.5→1.539 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.283 184 -
Rwork0.196 3302 -
obs--96.75 %

+
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