[English] 日本語
Yorodumi
- PDB-6woh: Diphosphoinositol polyphosphate phosphohydrolase 1 (DIPP1/NUDT3) ... -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 6woh
TitleDiphosphoinositol polyphosphate phosphohydrolase 1 (DIPP1/NUDT3) in complex with 1,5-di-methylenebisphosphonate inositol tetrakisphosphate (1,5-PCP-IP4)
ComponentsDiphosphoinositol polyphosphate phosphohydrolase 1
KeywordsHYDROLASE / phosphatase / nudix / catalysis mechanism / Substrate Specificity / inositol / inositol pyrophosphate
Function / homology
Function and homology information


diphosphoinositol polyphosphate catabolic process / inositol diphosphate pentakisphosphate diphosphatase activity / inositol diphosphate tetrakisphosphate diphosphatase activity / diadenosine polyphosphate catabolic process / diadenosine hexaphosphate catabolic process / diadenosine pentaphosphate catabolic process / RNA decapping / diphosphoinositol polyphosphate metabolic process / endopolyphosphatase activity / adenosine 5'-(hexahydrogen pentaphosphate) catabolic process ...diphosphoinositol polyphosphate catabolic process / inositol diphosphate pentakisphosphate diphosphatase activity / inositol diphosphate tetrakisphosphate diphosphatase activity / diadenosine polyphosphate catabolic process / diadenosine hexaphosphate catabolic process / diadenosine pentaphosphate catabolic process / RNA decapping / diphosphoinositol polyphosphate metabolic process / endopolyphosphatase activity / adenosine 5'-(hexahydrogen pentaphosphate) catabolic process / bis(5'-adenosyl)-pentaphosphatase activity / bis(5'-adenosyl)-hexaphosphatase activity / diphosphoinositol-polyphosphate diphosphatase activity / diphosphoinositol-polyphosphate diphosphatase / Synthesis of pyrophosphates in the cytosol / m7G(5')pppN diphosphatase activity / Hydrolases; Acting on acid anhydrides; In phosphorus-containing anhydrides / cell-cell signaling / magnesium ion binding / nucleus / cytosol / cytoplasm
Similarity search - Function
NUDIX hydrolase, conserved site / Nudix box signature. / NUDIX domain / NUDIX hydrolase domain / Nudix hydrolase domain profile. / NUDIX hydrolase-like domain superfamily
Similarity search - Domain/homology
Chem-4WZ / Diphosphoinositol polyphosphate phosphohydrolase 1
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / FOURIER SYNTHESIS / Resolution: 1.7 Å
AuthorsZong, G.N. / Wang, H.C. / Shears, S.B.
Funding support United States, 1items
OrganizationGrant numberCountry
National Institutes of Health/National Institute of Environmental Health Sciences (NIH/NIEHS)1ZIAES080046-31 United States
CitationJournal: Faseb J. / Year: 2021
Title: New structural insights reveal an expanded reaction cycle for inositol pyrophosphate hydrolysis by human DIPP1.
Authors: Zong, G. / Jork, N. / Hostachy, S. / Fiedler, D. / Jessen, H.J. / Shears, S.B. / Wang, H.
History
DepositionApr 24, 2020Deposition site: RCSB / Processing site: RCSB
Revision 1.0Mar 3, 2021Provider: repository / Type: Initial release

-
Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

-
Assembly

Deposited unit
A: Diphosphoinositol polyphosphate phosphohydrolase 1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)20,5514
Polymers19,5431
Non-polymers1,0083
Water1,982110
1


  • Idetical with deposited unit
  • defined by author&software
  • Evidence: gel filtration
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
Unit cell
Length a, b, c (Å)45.537, 59.904, 62.653
Angle α, β, γ (deg.)90.000, 90.000, 90.000
Int Tables number19
Space group name H-MP212121

-
Components

#1: Protein Diphosphoinositol polyphosphate phosphohydrolase 1 / DIPP-1 / Diadenosine 5' / 5'''-P1 / P6-hexaphosphate hydrolase 1 / Nucleoside diphosphate-linked ...DIPP-1 / Diadenosine 5' / 5'''-P1 / P6-hexaphosphate hydrolase 1 / Nucleoside diphosphate-linked moiety X motif 3 / Nudix motif 3


Mass: 19542.922 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: NUDT3, DIPP, DIPP1 / Production host: Escherichia coli (E. coli)
References: UniProt: O95989, diphosphoinositol-polyphosphate diphosphatase, Hydrolases; Acting on acid anhydrides; In phosphorus-containing anhydrides
#2: Chemical ChemComp-4WZ / {[(1R,3S,4S,5R,6S)-2,4,5,6-tetrakis(phosphonooxy)cyclohexane-1,3-diyl]bis[oxy(hydroxyphosphoryl)methanediyl]}bis(phosphonic acid)


Mass: 816.049 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C8H24O28P8 / Feature type: SUBJECT OF INVESTIGATION
#3: Chemical ChemComp-SO4 / SULFATE ION / Sulfate


Mass: 96.063 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: SO4 / Feature type: SUBJECT OF INVESTIGATION
#4: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 110 / Source method: isolated from a natural source / Formula: H2O
Has ligand of interestY

-
Experimental details

-
Experiment

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

-
Sample preparation

CrystalDensity Matthews: 2.19 Å3/Da / Density % sol: 43.74 %
Crystal growTemperature: 293 K / Method: vapor diffusion, hanging drop / pH: 6
Details: 10% (w/v) PEG 8000, 10% (v/v) isopropanol, 200 mM Li2SO4, 75 mM NaAc, pH 5.5 and 25 mM HEPES, pH 7.0 and soaking in solution of 200 mM LiCl, 20% (w/v) PEG 8000, 20% (v/v) isopropanol, 100 mM ...Details: 10% (w/v) PEG 8000, 10% (v/v) isopropanol, 200 mM Li2SO4, 75 mM NaAc, pH 5.5 and 25 mM HEPES, pH 7.0 and soaking in solution of 200 mM LiCl, 20% (w/v) PEG 8000, 20% (v/v) isopropanol, 100 mM HEPES, pH 7.0, 20 mM MgCl2 and 80 mM NaF in present of 2mM 1,5-PCP-IP4

-
Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 22-ID / Wavelength: 1 Å
DetectorType: DECTRIS EIGER X 16M / Detector: PIXEL / Date: Jun 14, 2019
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 1.7→50 Å / Num. obs: 19240 / % possible obs: 98.6 % / Redundancy: 7.3 % / Rmerge(I) obs: 0.075 / Rpim(I) all: 0.027 / Rrim(I) all: 0.08 / Χ2: 0.89 / Net I/σ(I): 10.9 / Num. measured all: 140892
Reflection shell

Diffraction-ID: 1

Resolution (Å)Redundancy (%)Rmerge(I) obsNum. unique obsCC1/2Rpim(I) allRrim(I) allΧ2% possible all
1.7-1.737.60.7578990.9240.2750.8090.77496.1
1.73-1.767.40.569440.9270.2050.5990.77396.6
1.76-1.797.40.4459190.9620.1630.4760.80898
1.79-1.837.10.3689440.960.1380.3940.83498.5
1.83-1.877.10.3339330.960.1260.3580.87198.4
1.87-1.916.90.2869620.9720.110.3080.91498.8
1.91-1.966.20.2299480.9710.0940.2490.92999.4
1.96-2.026.10.1829520.9810.0730.1970.87999
2.02-2.0770.1549530.9870.0580.1660.88798.8
2.07-2.147.90.1359680.9890.0480.1440.92799.9
2.14-2.228.10.1169800.9890.0410.1240.951100
2.22-2.3180.19420.9950.0350.1060.94399.5
2.31-2.4180.0869900.9950.030.0920.9499.5
2.41-2.547.80.0829570.9930.0290.0870.94499.9
2.54-2.77.80.0729860.9960.0260.0760.914100
2.7-2.917.50.0659700.9960.0230.0690.96799.3
2.91-3.27.20.0599700.9950.0220.0630.93698.6
3.2-3.666.40.069640.9940.0240.0640.96496.4
3.66-4.617.40.05510010.9960.020.0590.92597.8
4.61-507.50.05210580.9960.0190.0560.72497.2

-
Processing

Software
NameVersionClassification
REFMAC5.8.0253refinement
SCALEPACKdata scaling
PDB_EXTRACT3.25data extraction
DENZOdata reduction
PHASERphasing
RefinementMethod to determine structure: FOURIER SYNTHESIS / Resolution: 1.7→31.35 Å / Cor.coef. Fo:Fc: 0.949 / Cor.coef. Fo:Fc free: 0.931 / SU B: 1.986 / SU ML: 0.066 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.114 / ESU R Free: 0.11 / Stereochemistry target values: MAXIMUM LIKELIHOOD
Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS U VALUES : REFINED INDIVIDUALLY
RfactorNum. reflection% reflectionSelection details
Rfree0.2161 813 4.8 %RANDOM
Rwork0.185 ---
obs0.1865 16142 87.02 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK
Displacement parametersBiso max: 75.31 Å2 / Biso mean: 17.066 Å2 / Biso min: 6.46 Å2
Baniso -1Baniso -2Baniso -3
1-0.75 Å2-0 Å20 Å2
2---0.27 Å20 Å2
3----0.49 Å2
Refinement stepCycle: final / Resolution: 1.7→31.35 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms1086 0 54 110 1250
Biso mean--41.49 32.25 -
Num. residues----134
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0090.0131196
X-RAY DIFFRACTIONr_bond_other_d0.0010.0181070
X-RAY DIFFRACTIONr_angle_refined_deg1.7381.6971641
X-RAY DIFFRACTIONr_angle_other_deg1.371.6012490
X-RAY DIFFRACTIONr_dihedral_angle_1_deg7.2715145
X-RAY DIFFRACTIONr_dihedral_angle_2_deg26.62821.17668
X-RAY DIFFRACTIONr_dihedral_angle_3_deg12.0115205
X-RAY DIFFRACTIONr_dihedral_angle_4_deg15.6121511
X-RAY DIFFRACTIONr_chiral_restr0.170.2156
X-RAY DIFFRACTIONr_gen_planes_refined0.0070.021302
X-RAY DIFFRACTIONr_gen_planes_other0.0010.02259
LS refinement shellResolution: 1.7→1.743 Å / Rfactor Rfree error: 0
RfactorNum. reflection% reflection
Rfree0.254 34 -
Rwork0.231 770 -
obs--57.39 %

+
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