[English] 日本語
Yorodumi
- PDB-4ii1: Crystal structure of the zinc finger of ZGPAT -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 4ii1
TitleCrystal structure of the zinc finger of ZGPAT
ComponentsZinc finger CCCH-type with G patch domain-containing protein
KeywordsTRANSCRIPTION / transcription regulation / structural genomics consortium / SGC
Function / homology
Function and homology information


negative regulation of epidermal growth factor-activated receptor activity / DNA-binding transcription repressor activity, RNA polymerase II-specific / sequence-specific DNA binding / DNA-binding transcription factor activity, RNA polymerase II-specific / DNA-binding transcription factor activity / RNA polymerase II cis-regulatory region sequence-specific DNA binding / negative regulation of DNA-templated transcription / chromatin / negative regulation of transcription by RNA polymerase II / nucleoplasm ...negative regulation of epidermal growth factor-activated receptor activity / DNA-binding transcription repressor activity, RNA polymerase II-specific / sequence-specific DNA binding / DNA-binding transcription factor activity, RNA polymerase II-specific / DNA-binding transcription factor activity / RNA polymerase II cis-regulatory region sequence-specific DNA binding / negative regulation of DNA-templated transcription / chromatin / negative regulation of transcription by RNA polymerase II / nucleoplasm / nucleus / metal ion binding / plasma membrane
Similarity search - Function
SH3 type barrels. - #1190 / E3 ligase, CCCH-type zinc finger / CCCH-type zinc finger / G-patch domain / G-patch domain profile. / G-patch domain / glycine rich nucleic binding domain / Zinc finger, CCCH-type superfamily / zinc finger / Zinc finger, CCCH-type ...SH3 type barrels. - #1190 / E3 ligase, CCCH-type zinc finger / CCCH-type zinc finger / G-patch domain / G-patch domain profile. / G-patch domain / glycine rich nucleic binding domain / Zinc finger, CCCH-type superfamily / zinc finger / Zinc finger, CCCH-type / Zinc finger C3H1-type profile. / SH3 type barrels. - #140 / SH3 type barrels. / Roll / Mainly Beta
Similarity search - Domain/homology
Zinc finger CCCH-type with G patch domain-containing protein
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / SAD / Resolution: 2.65 Å
AuthorsBian, C. / Tempel, W. / Dong, A. / Chao, X. / Fu, M. / Wernimont, A.K. / Bountra, C. / Weigelt, J. / Arrowsmith, C.H. / Edwards, A.M. ...Bian, C. / Tempel, W. / Dong, A. / Chao, X. / Fu, M. / Wernimont, A.K. / Bountra, C. / Weigelt, J. / Arrowsmith, C.H. / Edwards, A.M. / Min, J. / Structural Genomics Consortium (SGC)
CitationJournal: to be published
Title: Crystal structure of the zinc finger of ZGPAT
Authors: Bian, C. / Tempel, W. / Dong, A. / Chao, X. / Fu, M. / Wernimont, A.K. / Bountra, C. / Weigelt, J. / Arrowsmith, C.H. / Edwards, A.M. / Min, J.
History
DepositionDec 19, 2012Deposition site: RCSB / Processing site: RCSB
Revision 1.0Feb 13, 2013Provider: repository / Type: Initial release
Revision 1.1Feb 28, 2024Group: Data collection / Database references / Derived calculations
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_struct_conn_angle / struct_conn / struct_ref_seq_dif / struct_site
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_struct_conn_angle.ptnr1_auth_asym_id / _pdbx_struct_conn_angle.ptnr1_auth_comp_id / _pdbx_struct_conn_angle.ptnr1_auth_seq_id / _pdbx_struct_conn_angle.ptnr1_label_asym_id / _pdbx_struct_conn_angle.ptnr1_label_atom_id / _pdbx_struct_conn_angle.ptnr1_label_comp_id / _pdbx_struct_conn_angle.ptnr1_label_seq_id / _pdbx_struct_conn_angle.ptnr2_auth_asym_id / _pdbx_struct_conn_angle.ptnr2_label_asym_id / _pdbx_struct_conn_angle.ptnr3_auth_asym_id / _pdbx_struct_conn_angle.ptnr3_auth_comp_id / _pdbx_struct_conn_angle.ptnr3_auth_seq_id / _pdbx_struct_conn_angle.ptnr3_label_asym_id / _pdbx_struct_conn_angle.ptnr3_label_atom_id / _pdbx_struct_conn_angle.ptnr3_label_comp_id / _pdbx_struct_conn_angle.ptnr3_label_seq_id / _pdbx_struct_conn_angle.value / _struct_conn.pdbx_dist_value / _struct_conn.ptnr1_auth_asym_id / _struct_conn.ptnr1_auth_comp_id / _struct_conn.ptnr1_auth_seq_id / _struct_conn.ptnr1_label_asym_id / _struct_conn.ptnr1_label_atom_id / _struct_conn.ptnr1_label_comp_id / _struct_conn.ptnr1_label_seq_id / _struct_conn.ptnr2_auth_asym_id / _struct_conn.ptnr2_label_asym_id / _struct_ref_seq_dif.details / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id

-
Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

-
Assembly

Deposited unit
A: Zinc finger CCCH-type with G patch domain-containing protein
B: Zinc finger CCCH-type with G patch domain-containing protein
C: Zinc finger CCCH-type with G patch domain-containing protein
D: Zinc finger CCCH-type with G patch domain-containing protein
hetero molecules


Theoretical massNumber of molelcules
Total (without water)75,37327
Polymers75,1114
Non-polymers26223
Water00
1
A: Zinc finger CCCH-type with G patch domain-containing protein
hetero molecules


Theoretical massNumber of molelcules
Total (without water)18,8437
Polymers18,7781
Non-polymers656
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
2
B: Zinc finger CCCH-type with G patch domain-containing protein
hetero molecules


Theoretical massNumber of molelcules
Total (without water)18,8436
Polymers18,7781
Non-polymers655
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
3
C: Zinc finger CCCH-type with G patch domain-containing protein
hetero molecules


Theoretical massNumber of molelcules
Total (without water)18,8435
Polymers18,7781
Non-polymers654
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
4
D: Zinc finger CCCH-type with G patch domain-containing protein
hetero molecules


Theoretical massNumber of molelcules
Total (without water)18,8439
Polymers18,7781
Non-polymers658
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
Unit cell
Length a, b, c (Å)55.170, 87.070, 76.570
Angle α, β, γ (deg.)90.000, 95.650, 90.000
Int Tables number4
Space group name H-MP1211

-
Components

#1: Protein
Zinc finger CCCH-type with G patch domain-containing protein / G patch domain-containing protein 6 / Zinc finger CCCH domain-containing protein 9 / Zinc finger ...G patch domain-containing protein 6 / Zinc finger CCCH domain-containing protein 9 / Zinc finger and G patch domain-containing protein


Mass: 18777.736 Da / Num. of mol.: 4 / Fragment: UNP residues 119-268
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: ZGPAT, GPATC6, GPATCH6, KIAA1847, ZC3H9, ZC3HDC9, ZIP / Plasmid: pET28-MHL / Production host: Escherichia coli (E. coli) / Strain (production host): BL21 / References: UniProt: Q8N5A5
#2: Chemical
ChemComp-ZN / ZINC ION


Mass: 65.409 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: Zn
#3: Chemical
ChemComp-UNX / UNKNOWN ATOM OR ION


Num. of mol.: 19 / Source method: obtained synthetically

-
Experimental details

-
Experiment

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

-
Sample preparation

CrystalDensity Matthews: 2.44 Å3/Da / Density % sol: 49.52 %
Crystal growTemperature: 291 K / Method: vapor diffusion, sitting drop / pH: 7.5
Details: 1.2 M sodium citrate, 5% MPD, 0.1 M sodium HEPES, 3 molar equivalents of H3K4me3 peptide., pH 7.5, vapor diffusion, sitting drop, temperature 291K

-
Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 23-ID-B / Wavelength: 1.28292 Å
DetectorType: MAR scanner 300 mm plate / Detector: IMAGE PLATE / Date: Apr 8, 2011
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.28292 Å / Relative weight: 1
ReflectionResolution: 2.65→37.8 Å / Num. obs: 20804 / % possible obs: 98.7 % / Observed criterion σ(I): -3 / Biso Wilson estimate: 67.802 Å2 / Rmerge(I) obs: 0.073 / Net I/σ(I): 12.55
Reflection shell

Diffraction-ID: 1

Resolution (Å)Highest resolution (Å)Rmerge(I) obsMean I/σ(I) obsNum. measured obsNum. unique obs% possible all
2.65-2.720.9461.946400151998.3
2.72-2.790.7442.316311148198.7
2.79-2.870.5383.116160144498.8
2.87-2.960.3924.026012141298.9
2.96-3.060.3174.845979140598.7
3.06-3.170.2256.445521128998.8
3.17-3.290.1668.435468128899.2
3.29-3.420.11710.795248123799.5
3.42-3.570.10412.444979117598.7
3.57-3.750.07615.214707112698.8
3.75-3.950.06118.164585109399.3
3.95-4.190.04920.894267101799
4.19-4.480.04623.12399896599.3
4.48-4.840.04224.19370790499.3
4.84-5.30.04325.21336181899.4
5.3-5.930.04824.41307975799.5
5.93-6.840.05124.42263266498.7
6.84-8.380.04826.23220555597.2
8.38-11.850.04228.22166543197.1
11.850.03727.6481922486.2

-
Processing

Software
NameVersionClassificationNB
XSCALEdata scaling
SHELXphasing
SHARPphasing
BUSTER-TNTBUSTER 2.10.0refinement
PDB_EXTRACT3.11data extraction
XDSdata reduction
BUSTER2.10.0refinement
RefinementMethod to determine structure: SAD / Resolution: 2.65→37.8 Å / Cor.coef. Fo:Fc: 0.918 / Cor.coef. Fo:Fc free: 0.8855 / Occupancy max: 1 / Occupancy min: 0.5 / SU R Cruickshank DPI: 0.494 / Cross valid method: THROUGHOUT / σ(F): 0
Details: DM, resolve, refmac, buccaneer, arp/warp atom update, PARROT, PHASER were also used for phase improvement and model building/refinement. COOT was used for interactive model re-building and ...Details: DM, resolve, refmac, buccaneer, arp/warp atom update, PARROT, PHASER were also used for phase improvement and model building/refinement. COOT was used for interactive model re-building and model geometry was validated on the MOLPROBITY server.
RfactorNum. reflection% reflectionSelection details
Rfree0.2416 985 4.74 %THIN SHELLS (SFTOOLS)
Rwork0.2085 ---
obs0.2102 20787 98.76 %-
Displacement parametersBiso max: 163.14 Å2 / Biso mean: 66.9971 Å2 / Biso min: 30 Å2
Baniso -1Baniso -2Baniso -3
1-9.6709 Å20 Å24.6329 Å2
2---12.7657 Å20 Å2
3---3.0948 Å2
Refine analyzeLuzzati coordinate error obs: 0.347 Å
Refinement stepCycle: LAST / Resolution: 2.65→37.8 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms3947 0 23 0 3970
Refine LS restraints
Refine-IDTypeNumberRestraint functionWeightDev ideal
X-RAY DIFFRACTIONt_dihedral_angle_d1225SINUSOIDAL2
X-RAY DIFFRACTIONt_trig_c_planes71HARMONIC2
X-RAY DIFFRACTIONt_gen_planes622HARMONIC5
X-RAY DIFFRACTIONt_it4054HARMONIC20
X-RAY DIFFRACTIONt_nbd0SEMIHARMONIC5
X-RAY DIFFRACTIONt_improper_torsion
X-RAY DIFFRACTIONt_pseud_angle
X-RAY DIFFRACTIONt_chiral_improper_torsion530SEMIHARMONIC5
X-RAY DIFFRACTIONt_sum_occupancies
X-RAY DIFFRACTIONt_utility_distance16HARMONIC1
X-RAY DIFFRACTIONt_utility_angle
X-RAY DIFFRACTIONt_utility_torsion
X-RAY DIFFRACTIONt_ideal_dist_contact4025SEMIHARMONIC4
X-RAY DIFFRACTIONt_bond_d4054HARMONIC20.009
X-RAY DIFFRACTIONt_angle_deg5540HARMONIC21.01
X-RAY DIFFRACTIONt_omega_torsion2.65
X-RAY DIFFRACTIONt_other_torsion18.52
LS refinement shellResolution: 2.65→2.79 Å / Total num. of bins used: 10
RfactorNum. reflection% reflection
Rfree0.2388 147 4.9 %
Rwork0.2299 2850 -
all0.2304 2997 -
obs--98.76 %

+
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