[English] 日本語
Yorodumi
- EMDB-64458: apo form of polyphosphate kinase 1 (PPK1) -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: EMDB / ID: EMD-64458
Titleapo form of polyphosphate kinase 1 (PPK1)
Map data
Sample
  • Complex: apo form of polyphosphate kinase 1 (PPK1)
    • Protein or peptide: Polyphosphate kinase
KeywordsCryo-EM / transferase
Function / homology
Function and homology information


diphosphotransferase activity / polyphosphate:AMP phosphotransferase activity / polyphosphate kinase complex / ATP-polyphosphate phosphotransferase / polyphosphate biosynthetic process / periplasmic side of cell outer membrane / polyphosphate kinase activity / phosphotransferase activity, phosphate group as acceptor / regulation of cell division / protein homodimerization activity ...diphosphotransferase activity / polyphosphate:AMP phosphotransferase activity / polyphosphate kinase complex / ATP-polyphosphate phosphotransferase / polyphosphate biosynthetic process / periplasmic side of cell outer membrane / polyphosphate kinase activity / phosphotransferase activity, phosphate group as acceptor / regulation of cell division / protein homodimerization activity / ATP binding / metal ion binding / membrane / plasma membrane / cytosol
Similarity search - Function
Polyphosphate kinase / Polyphosphate kinase middle domain / Polyphosphate kinase N-terminal domain / Polyphosphate kinase C-terminal domain 2 / Polyphosphate kinase middle domain superfamily / Polyphosphate kinase N-terminal domain superfamily / Polyphosphate kinase, C-terminal domain 1 / Polyphosphate kinase middle domain / Polyphosphate kinase N-terminal domain / Polyphosphate kinase C-terminal domain 2 ...Polyphosphate kinase / Polyphosphate kinase middle domain / Polyphosphate kinase N-terminal domain / Polyphosphate kinase C-terminal domain 2 / Polyphosphate kinase middle domain superfamily / Polyphosphate kinase N-terminal domain superfamily / Polyphosphate kinase, C-terminal domain 1 / Polyphosphate kinase middle domain / Polyphosphate kinase N-terminal domain / Polyphosphate kinase C-terminal domain 2 / Polyphosphate kinase C-terminal domain 1 / Phospholipase D/Transphosphatidylase / Phospholipase D phosphodiesterase active site profile.
Similarity search - Domain/homology
Polyphosphate kinase
Similarity search - Component
Biological speciesEscherichia coli (strain K12) (bacteria)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.09 Å
AuthorsJiang WJ / Zhao J / Wei W
Funding support1 items
OrganizationGrant numberCountry
Not funded
CitationJournal: To Be Published
Title: Structural Insights into PPK1 Catalyzed Triple Phosphoryl Transfer Underlying Polyphosphate Biosynthesis
Authors: Jiang WJ / Zhao J / Wei W
History
DepositionApr 30, 2025-
Header (metadata) releaseMar 4, 2026-
Map releaseMar 4, 2026-
UpdateMar 4, 2026-
Current statusMar 4, 2026Processing site: PDBc / Status: Released

-
Structure visualization

Supplemental images

Downloads & links

-
Map

FileDownload / File: emd_64458.map.gz / Format: CCP4 / Size: 244.1 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
0.74 Å/pix.
x 400 pix.
= 297.2 Å
0.74 Å/pix.
x 400 pix.
= 297.2 Å
0.74 Å/pix.
x 400 pix.
= 297.2 Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 0.743 Å
Density
Contour LevelBy AUTHOR: 0.155
Minimum - Maximum-0.6523761 - 0.92110777
Average (Standard dev.)0.0007675088 (±0.028304271)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions400400400
Spacing400400400
CellA=B=C: 297.19998 Å
α=β=γ: 90.0 °

-
Supplemental data

-
Mask #1

Fileemd_64458_msk_1.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

-
Half map: #2

Fileemd_64458_half_map_1.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

-
Half map: #1

Fileemd_64458_half_map_2.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

-
Sample components

-
Entire : apo form of polyphosphate kinase 1 (PPK1)

EntireName: apo form of polyphosphate kinase 1 (PPK1)
Components
  • Complex: apo form of polyphosphate kinase 1 (PPK1)
    • Protein or peptide: Polyphosphate kinase

-
Supramolecule #1: apo form of polyphosphate kinase 1 (PPK1)

SupramoleculeName: apo form of polyphosphate kinase 1 (PPK1) / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all
Source (natural)Organism: Escherichia coli (strain K12) (bacteria)

-
Macromolecule #1: Polyphosphate kinase

MacromoleculeName: Polyphosphate kinase / type: protein_or_peptide / ID: 1 / Number of copies: 4 / Enantiomer: LEVO / EC number: ATP-polyphosphate phosphotransferase
Source (natural)Organism: Escherichia coli (strain K12) (bacteria)
Molecular weightTheoretical: 80.079898 KDa
Recombinant expressionOrganism: Escherichia coli BL21(DE3) (bacteria)
SequenceString: EKLYIEKELS WLSFNERVLQ EAADKSNPLI ERMRFLGIYS NNLDEFYKVR FAELKRRIII SEEQGSNSHS RHLLGKIQSR VLKADQEFD GLYNELLLEM ARNQIFLINE RQLSVNQQNW LRHYFKQYLR QHITPILINP DTDLVQFLKD DYTYLAVEII R GDTIRYAL ...String:
EKLYIEKELS WLSFNERVLQ EAADKSNPLI ERMRFLGIYS NNLDEFYKVR FAELKRRIII SEEQGSNSHS RHLLGKIQSR VLKADQEFD GLYNELLLEM ARNQIFLINE RQLSVNQQNW LRHYFKQYLR QHITPILINP DTDLVQFLKD DYTYLAVEII R GDTIRYAL LEIPSDKVPR FVNLPPEAPR RRKPMILLDN ILRYCLDDIF KGFFDYDALN AYSMKMTRDA EYDLVHEMEA SL MELMSSS LKQRLTAEPV RFVYQRDMPN ALVEVLREKL TISRYDSIVP GGRYHNFKDF INFPNVGKAN LVNKPLPRLR HIW FDKAQF RNGFDAIRER DVLLYYPYHT FEHVLELLRQ ASFDPSVLAI KINIYRVAKD SRIIDSMIHA AHNGKKVTVV VELQ ARFDE EANIHWAKRL TEAGVHVIFS APGLKIQAKL FLISRKENGE VVRYAHIGTG NFNEKTARLY TDYSLLTADA RITNE VRRV FNFIENPYRP VTFDYLMVSP QNSRRLLYEM VDREIANAQQ GLPSGITLKL NNLVDKGLVD RLYAASSSGV PVNLLV RGM CSLIPNLEGI SDNIRAISIV DRYLEQDRVY IFENGGDKKV YLSSADWMTR NIDYRIEVAT PLLDPRLKQR VLDIIDI LF SDTVKARYID KELSNRYVPR GNRRKVRAQL AIYDYIKSLE QP

UniProtKB: Polyphosphate kinase

-
Experimental details

-
Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation stateparticle

-
Sample preparation

BufferpH: 7.5
VitrificationCryogen name: ETHANE

-
Electron microscopy

MicroscopeTFS KRIOS
Image recordingFilm or detector model: FEI FALCON IV (4k x 4k) / Average electron dose: 55.0 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.4 µm / Nominal defocus min: 1.0 µm
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

+
Image processing

CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
Startup modelType of model: OTHER / Details: From cryoSPARC Ab-initio reconstruction
Final reconstructionResolution.type: BY AUTHOR / Resolution: 3.09 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 35020
Initial angle assignmentType: MAXIMUM LIKELIHOOD
Final angle assignmentType: MAXIMUM LIKELIHOOD
FSC plot (resolution estimation)

+
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