[English] 日本語
Yorodumi
- PDB-4wzr: Crystal structure of human Puf-A -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 4wzr
TitleCrystal structure of human Puf-A
ComponentsPumilio domain-containing protein KIAA0020
KeywordsRNA BINDING PROTEIN / Pumilio repeat protein
Function / homology
Function and homology information


regulation of protein ADP-ribosylation / regulation of translation / chromosome / mRNA binding / nucleolus / endoplasmic reticulum / DNA binding / RNA binding / nucleoplasm
Similarity search - Function
CPL domain / Pumilio homologue 3 / CPL (NUC119) domain / Pumilio homology domain / Pumilio homology domain (PUM-HD) profile. / Pumilio RNA-binding repeat profile. / Pumilio RNA-binding repeat / Pumilio-like repeats / Armadillo-like helical / Armadillo-type fold
Similarity search - Domain/homology
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / SAD / Resolution: 2.154 Å
AuthorsQiu, C. / Hall, T.M.T.
Funding support United States, 1items
OrganizationGrant numberCountry
National Institutes of Health/National Institute of Environmental Health Sciences (NIH/NIEHS)Intramural Research Program United States
CitationJournal: Proc.Natl.Acad.Sci.USA / Year: 2014
Title: A divergent Pumilio repeat protein family for pre-rRNA processing and mRNA localization.
Authors: Qiu, C. / McCann, K.L. / Wine, R.N. / Baserga, S.J. / Hall, T.M.
History
DepositionNov 20, 2014Deposition site: RCSB / Processing site: RCSB
Revision 1.0Dec 31, 2014Provider: repository / Type: Initial release
Revision 1.1Jan 14, 2015Group: Database references
Revision 1.2Feb 4, 2015Group: Derived calculations
Revision 1.3Nov 27, 2019Group: Author supporting evidence / Database references ...Author supporting evidence / Database references / Derived calculations / Source and taxonomy
Category: citation / entity_src_gen ...citation / entity_src_gen / pdbx_audit_support / pdbx_struct_oper_list
Item: _citation.journal_id_CSD / _entity_src_gen.pdbx_alt_source_flag ..._citation.journal_id_CSD / _entity_src_gen.pdbx_alt_source_flag / _pdbx_audit_support.funding_organization / _pdbx_struct_oper_list.symmetry_operation
Revision 1.4Feb 28, 2024Group: Data collection / Database references / Category: chem_comp_atom / chem_comp_bond / database_2
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession

-
Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

-
Assembly

Deposited unit
A: Pumilio domain-containing protein KIAA0020
B: Pumilio domain-containing protein KIAA0020
hetero molecules


Theoretical massNumber of molelcules
Total (without water)119,5134
Polymers119,3292
Non-polymers1842
Water7,116395
1
A: Pumilio domain-containing protein KIAA0020
hetero molecules


Theoretical massNumber of molelcules
Total (without water)59,7562
Polymers59,6641
Non-polymers921
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
2
B: Pumilio domain-containing protein KIAA0020
hetero molecules


Theoretical massNumber of molelcules
Total (without water)59,7562
Polymers59,6641
Non-polymers921
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
Unit cell
Length a, b, c (Å)93.495, 97.128, 282.801
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number20
Space group name H-MC2221
Components on special symmetry positions
IDModelComponents
11B-818-

HOH

-
Components

#1: Protein Pumilio domain-containing protein KIAA0020 / HBV X-transactivated gene 5 protein / HBV XAg-transactivated protein 5 / Minor histocompatibility ...HBV X-transactivated gene 5 protein / HBV XAg-transactivated protein 5 / Minor histocompatibility antigen HA-8 / HLA-HA8 / Puf-A


Mass: 59664.340 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: KIAA0020, XTP5 / Production host: Escherichia coli (E. coli) / References: UniProt: Q15397
#2: Chemical ChemComp-GOL / GLYCEROL / GLYCERIN / PROPANE-1,2,3-TRIOL / Glycerol


Mass: 92.094 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C3H8O3
#3: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 395 / 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: 2.72 Å3/Da / Density % sol: 54.73 %
Crystal growTemperature: 293 K / Method: vapor diffusion, hanging drop / Details: 20-25% PEG 3350, 0.2 M sodium malonate / PH range: 7

-
Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 22-ID / Wavelength: 0.979 Å
DetectorType: MARMOSAIC 300 mm CCD / Detector: CCD / Date: Nov 2, 2011
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.979 Å / Relative weight: 1
ReflectionResolution: 2.15→50 Å / Num. obs: 68219 / % possible obs: 97.9 % / Redundancy: 7 % / Rsym value: 0.093 / Net I/σ(I): 19
Reflection shellResolution: 2.15→2.93 Å / Redundancy: 4.9 % / Rmerge(I) obs: 0.458 / Mean I/σ(I) obs: 2.8 / % possible all: 84.2

-
Processing

Software
NameVersionClassification
PHENIX(phenix.refine: 1.8.2_1309)refinement
HKL-2000data reduction
HKL-2000data scaling
PHENIXphasing
RefinementMethod to determine structure: SAD / Resolution: 2.154→48.564 Å / SU ML: 0.23 / Cross valid method: FREE R-VALUE / σ(F): 1.34 / Phase error: 22.79 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2265 1998 2.93 %
Rwork0.1798 --
obs0.1811 68195 97.59 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.2 Å / Solvent model: FLAT BULK SOLVENT MODEL
Refinement stepCycle: LAST / Resolution: 2.154→48.564 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms8145 0 12 395 8552
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0078331
X-RAY DIFFRACTIONf_angle_d1.02211224
X-RAY DIFFRACTIONf_dihedral_angle_d13.1333219
X-RAY DIFFRACTIONf_chiral_restr0.0661294
X-RAY DIFFRACTIONf_plane_restr0.0041412
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2.1543-2.20820.26941210.22653882X-RAY DIFFRACTION81
2.2082-2.26790.25461280.21174489X-RAY DIFFRACTION93
2.2679-2.33470.25071420.20374681X-RAY DIFFRACTION97
2.3347-2.410.27391470.19474710X-RAY DIFFRACTION99
2.41-2.49620.24261440.19284780X-RAY DIFFRACTION99
2.4962-2.59610.24661490.19224791X-RAY DIFFRACTION99
2.5961-2.71420.24051390.18894733X-RAY DIFFRACTION99
2.7142-2.85730.25841390.19464797X-RAY DIFFRACTION99
2.8573-3.03630.24481420.20664846X-RAY DIFFRACTION100
3.0363-3.27070.271460.19994788X-RAY DIFFRACTION100
3.2707-3.59970.24221460.17864858X-RAY DIFFRACTION100
3.5997-4.12040.20461490.16184859X-RAY DIFFRACTION100
4.1204-5.19030.18571460.15214929X-RAY DIFFRACTION100
5.1903-48.57630.20021600.1695054X-RAY DIFFRACTION100
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)
17.9121.6108-3.93437.593-2.76015.00950.20610.09480.17530.4594-0.26380.28420.1307-0.16240.05670.3284-0.1181-0.03690.3341-0.02070.219987.2827105.6805161.8787
22.90380.81441.94021.14040.95951.5836-0.1205-0.07260.1225-0.15350.0516-0.0736-0.2530.02280.06280.4352-0.11010.06880.3222-0.0010.222961.910284.7645163.0667
31.7688-0.9111-1.83011.2251.46333.7052-0.04190.196-0.138-0.15750.0798-0.0796-0.12710.2357-0.02520.325-0.1550.02340.4434-0.03340.230962.307364.636126.9857
47.96590.5331-0.48061.80620.1865.0129-0.3174-0.0425-0.3024-0.34740.22840.42530.00180.06830.0950.3721-0.0996-0.13560.2854-0.01140.6016106.791792.147355.8592
52.17682.38090.4692.61690.41930.3152-0.41520.30060.15280.31330.1387-1.4074-0.21270.19110.18830.4207-0.0528-0.19610.33940.00820.717793.954680.945650.6286
60.94740.6391-0.70541.7961-1.26852.5597-0.07870.12960.008-0.13540.0286-0.00770.0689-0.09110.05010.1821-0.0443-0.02420.2616-0.05390.208279.327659.555457.1617
71.8679-0.2812-1.84260.62150.87973.34840.2875-0.20150.14260.0304-0.13120.1542-0.4549-0.0687-0.12080.3907-0.1220.04460.3079-0.0510.247860.469963.957791.5019
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1chain 'A' and (resid 131 through 211 )
2X-RAY DIFFRACTION2chain 'A' and (resid 212 through 374 )
3X-RAY DIFFRACTION3chain 'A' and (resid 375 through 646 )
4X-RAY DIFFRACTION4chain 'B' and (resid 127 through 179 )
5X-RAY DIFFRACTION5chain 'B' and (resid 180 through 248 )
6X-RAY DIFFRACTION6chain 'B' and (resid 249 through 399 )
7X-RAY DIFFRACTION7chain 'B' and (resid 400 through 646 )

+
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