[English] 日本語
Yorodumi
- PDB-9igq: Crystal structure of PPK2 class III from Erysipelotrichaceae bact... -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 9igq
TitleCrystal structure of PPK2 class III from Erysipelotrichaceae bacterium in complex with AppCH2p and polyphosphate
ComponentsPolyphosphate--nucleotide phosphotransferase
KeywordsTRANSFERASE / Polyphosphate Kinase / PPK2-III / NTP / EbPPK
Function / homology
Function and homology information


polyphosphate kinase activity / polyphosphate metabolic process
Similarity search - Function
Polyphosphate:nucleotide phosphotransferase, PPK2 / Polyphosphate phosphotransferase / Polyphosphate kinase-2-related / Polyphosphate kinase 2 (PPK2) / P-loop containing nucleoside triphosphate hydrolase
Similarity search - Domain/homology
Chem-6YY / : / PHOSPHOMETHYLPHOSPHONIC ACID ADENYLATE ESTER / BENZOIC ACID / Polyphosphate--nucleotide phosphotransferase
Similarity search - Component
Biological speciesErysipelotrichaceae bacterium (bacteria)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.7 Å
AuthorsRasche, R. / Lawrence-Doerner, A.-M. / Cornelissen, N.V. / Kuemmel, D.
Funding support1items
OrganizationGrant numberCountry
Not funded
CitationJournal: Rsc Chem Biol / Year: 2025
Title: Structure-guided engineering of a polyphosphate kinase 2 class III from an Erysipelotrichaceae bacterium to produce base-modified purine nucleotides
Authors: Mitton-Fry, R.M. / Rasche, R. / Lawrence-Dorner, A.M. / Eschenbach, J. / Tekath, A. / Rentmeister, A. / Kummel, D. / Cornelissen, N.V.
History
DepositionFeb 20, 2025Deposition site: PDBE / Processing site: PDBE
Revision 1.0Jul 23, 2025Provider: repository / Type: Initial release

-
Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

-
Assembly

Deposited unit
A: Polyphosphate--nucleotide phosphotransferase
B: Polyphosphate--nucleotide phosphotransferase
C: Polyphosphate--nucleotide phosphotransferase
D: Polyphosphate--nucleotide phosphotransferase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)152,40728
Polymers146,5014
Non-polymers5,90624
Water18,1591008
1


  • Idetical with deposited unit
  • defined by author
  • Evidence: gel filtration
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area22910 Å2
ΔGint-164 kcal/mol
Surface area47970 Å2
Unit cell
Length a, b, c (Å)77.888, 110.734, 152.585
Angle α, β, γ (deg.)90, 90, 90
Int Tables number19
Space group name H-MP212121
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11A
21B
32A
42C
53A
63D
74B
84C
95B
105D
116C
126D

NCS domain segments:
Dom-IDComponent-IDEns-IDBeg auth comp-IDBeg label comp-IDEnd auth comp-IDEnd label comp-IDAuth asym-IDLabel asym-IDAuth seq-IDLabel seq-ID
111ASNASNPROPROAA3 - 2953 - 295
211ASNASNPROPROBB3 - 2953 - 295
322ASNASNASPASPAA3 - 2893 - 289
422ASNASNASPASPCC3 - 2893 - 289
533ASNASNTYRTYRAA3 - 2883 - 288
633ASNASNTYRTYRDD3 - 2883 - 288
744ASNASNASPASPBB3 - 2893 - 289
844ASNASNASPASPCC3 - 2893 - 289
955ALAALATYRTYRBB2 - 2882 - 288
1055ALAALATYRTYRDD2 - 2882 - 288
1166ASNASNTYRTYRCC3 - 2883 - 288
1266ASNASNTYRTYRDD3 - 2883 - 288

NCS ensembles :
IDDetails
1Local NCS retraints between domains: 1 2
2Local NCS retraints between domains: 3 4
3Local NCS retraints between domains: 5 6
4Local NCS retraints between domains: 7 8
5Local NCS retraints between domains: 9 10
6Local NCS retraints between domains: 11 12

-
Components

-
Protein , 1 types, 4 molecules ABCD

#1: Protein
Polyphosphate--nucleotide phosphotransferase


Mass: 36625.246 Da / Num. of mol.: 4 / Mutation: I2A
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Erysipelotrichaceae bacterium (bacteria)
Strain: UBA9076 / Gene: DHS57_05705
Production host: Escherichia coli 'BL21-Gold(DE3)pLysS AG' (bacteria)
References: UniProt: A0A3D5XRJ5

-
Non-polymers , 8 types, 1032 molecules

#2: Chemical
ChemComp-ACP / PHOSPHOMETHYLPHOSPHONIC ACID ADENYLATE ESTER / ADENOSINE-5'-[BETA, GAMMA-METHYLENE]TRIPHOSPHATE


Mass: 505.208 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C11H18N5O12P3 / Feature type: SUBJECT OF INVESTIGATION / Comment: AMP-PCP, energy-carrying molecule analogue*YM
#3: Chemical ChemComp-6YY / bis[oxidanyl-[oxidanyl-[oxidanyl-[oxidanyl(phosphonooxy)phosphoryl]oxy-phosphoryl]oxy-phosphoryl]oxy-phosphoryl] hydrogen phosphate


Mass: 897.794 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: H13O34P11 / Feature type: SUBJECT OF INVESTIGATION
#4: Chemical ChemComp-GOL / GLYCEROL / GLYCERIN / PROPANE-1,2,3-TRIOL


Mass: 92.094 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C3H8O3
#5: Chemical ChemComp-BEZ / BENZOIC ACID


Mass: 122.121 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C7H6O2
#6: Chemical
ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 10 / Source method: obtained synthetically / Formula: Mg
#7: Chemical ChemComp-MPD / (4S)-2-METHYL-2,4-PENTANEDIOL


Mass: 118.174 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: C6H14O2 / Comment: precipitant*YM
#8: Chemical ChemComp-A1I4D / bis[oxidanyl-[oxidanyl(phosphonooxy)phosphoryl]oxy-phosphoryl] hydrogen phosphate


Mass: 577.875 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: H9O22P7 / Feature type: SUBJECT OF INVESTIGATION
#9: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 1008 / Source method: isolated from a natural source / Formula: H2O

-
Details

Has ligand of interestY
Has protein modificationN

-
Experimental details

-
Experiment

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

-
Sample preparation

CrystalDensity Matthews: 2.32 Å3/Da / Density % sol: 46.97 %
Crystal growTemperature: 285 K / Method: vapor diffusion, sitting drop / pH: 4.6
Details: MPD 20%, sodium acetate 0.1 M, sodium chloride 0.2 M

-
Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: PETRA III, EMBL c/o DESY / Beamline: P13 (MX1) / Wavelength: 0.976 Å
DetectorType: DECTRIS EIGER X 16M / Detector: PIXEL / Date: Sep 15, 2024
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.976 Å / Relative weight: 1
ReflectionResolution: 1.7→48.9 Å / Num. obs: 145127 / % possible obs: 98.4 % / Redundancy: 13.7 % / Biso Wilson estimate: 18.53 Å2 / CC1/2: 0.998 / CC star: 0.999 / Rpim(I) all: 0.0533 / Rrim(I) all: 0.193 / Net I/σ(I): 10.76
Reflection shellResolution: 1.7→1.8 Å / Redundancy: 12.5 % / Mean I/σ(I) obs: 1.51 / Num. unique obs: 23262 / CC1/2: 0.635 / CC star: 0.878 / Rpim(I) all: 0.593 / Rrim(I) all: 2.15 / % possible all: 99.8

-
Processing

Software
NameVersionClassification
REFMAC5.8.0430 (refmacat 0.4.88)refinement
XDSdata reduction
XDSdata scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT / Resolution: 1.7→48.9 Å / Cor.coef. Fo:Fc: 0.972 / Cor.coef. Fo:Fc free: 0.965 / SU B: 5.289 / SU ML: 0.083 / Cross valid method: FREE R-VALUE / ESU R: 0.101 / ESU R Free: 0.097
Details: Hydrogens have been added in their riding positions
RfactorNum. reflection% reflection
Rfree0.1969 7180 4.968 %
Rwork0.1671 137349 -
all0.169 --
obs-144529 99.467 %
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK BULK SOLVENT
Displacement parametersBiso mean: 30.49 Å2
Baniso -1Baniso -2Baniso -3
1--0.228 Å20 Å20 Å2
2--0.946 Å2-0 Å2
3----0.717 Å2
Refinement stepCycle: LAST / Resolution: 1.7→48.9 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms9812 0 330 1008 11150
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0140.01210422
X-RAY DIFFRACTIONr_bond_other_d0.0020.0169576
X-RAY DIFFRACTIONr_angle_refined_deg2.2111.87314171
X-RAY DIFFRACTIONr_angle_other_deg0.8141.80522104
X-RAY DIFFRACTIONr_dihedral_angle_1_deg5.9551181
X-RAY DIFFRACTIONr_dihedral_angle_2_deg6.688560
X-RAY DIFFRACTIONr_dihedral_angle_other_2_deg1.16154
X-RAY DIFFRACTIONr_dihedral_angle_3_deg13.05101886
X-RAY DIFFRACTIONr_dihedral_angle_6_deg15.73710554
X-RAY DIFFRACTIONr_chiral_restr0.1120.21507
X-RAY DIFFRACTIONr_gen_planes_refined0.0120.0211952
X-RAY DIFFRACTIONr_gen_planes_other0.0030.022420
X-RAY DIFFRACTIONr_nbd_refined0.210.22043
X-RAY DIFFRACTIONr_symmetry_nbd_other0.1550.28496
X-RAY DIFFRACTIONr_nbtor_refined0.1820.25026
X-RAY DIFFRACTIONr_symmetry_nbtor_other0.0730.25524
X-RAY DIFFRACTIONr_xyhbond_nbd_refined0.1380.2783
X-RAY DIFFRACTIONr_symmetry_nbd_refined0.340.232
X-RAY DIFFRACTIONr_nbd_other0.2140.266
X-RAY DIFFRACTIONr_symmetry_xyhbond_nbd_refined0.1740.226
X-RAY DIFFRACTIONr_mcbond_it2.3961.6734688
X-RAY DIFFRACTIONr_mcbond_other2.3931.6734688
X-RAY DIFFRACTIONr_mcangle_it3.5012.9935863
X-RAY DIFFRACTIONr_mcangle_other3.5012.9945864
X-RAY DIFFRACTIONr_scbond_it4.7042.235734
X-RAY DIFFRACTIONr_scbond_other4.7032.235735
X-RAY DIFFRACTIONr_scangle_it6.9363.9248302
X-RAY DIFFRACTIONr_scangle_other6.9353.9248303
X-RAY DIFFRACTIONr_lrange_it8.35520.01712187
X-RAY DIFFRACTIONr_lrange_other8.33619.4711924
X-RAY DIFFRACTIONr_ncsr_local_group_10.0630.0510017
X-RAY DIFFRACTIONr_ncsr_local_group_20.0830.059717
X-RAY DIFFRACTIONr_ncsr_local_group_30.0860.059662
X-RAY DIFFRACTIONr_ncsr_local_group_40.0860.059677
X-RAY DIFFRACTIONr_ncsr_local_group_50.0910.059646
X-RAY DIFFRACTIONr_ncsr_local_group_60.0770.059895
Refine LS restraints NCS
Ens-IDDom-IDAuth asym-IDRefine-IDTypeRms dev position (Å)Weight position
11AX-RAY DIFFRACTIONLocal ncs0.063040.05008
12BX-RAY DIFFRACTIONLocal ncs0.063040.05008
23AX-RAY DIFFRACTIONLocal ncs0.082880.05008
24CX-RAY DIFFRACTIONLocal ncs0.082880.05008
35AX-RAY DIFFRACTIONLocal ncs0.085540.05008
36DX-RAY DIFFRACTIONLocal ncs0.085540.05008
47BX-RAY DIFFRACTIONLocal ncs0.085760.05008
48CX-RAY DIFFRACTIONLocal ncs0.085760.05008
59BX-RAY DIFFRACTIONLocal ncs0.09130.05008
510DX-RAY DIFFRACTIONLocal ncs0.09130.05008
611CX-RAY DIFFRACTIONLocal ncs0.077350.05008
612DX-RAY DIFFRACTIONLocal ncs0.077350.05008
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Total num. of bins used: 20

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRfactor allNum. reflection allFsc freeFsc work% reflection obs (%)WRfactor Rwork
1.7-1.7440.2955430.292100380.292105850.9380.94199.96220.275
1.744-1.7920.2765370.25898220.259103660.9460.95299.93250.24
1.792-1.8440.2644750.2496070.241100940.9510.95999.88110.219
1.844-1.90.274820.23292810.23497880.9510.96499.74460.205
1.9-1.9630.3194900.27889090.2895180.9480.9698.74970.246
1.963-2.0310.3524320.29884800.30191750.9440.95997.13350.251
2.031-2.1080.314430.27182520.27388920.9570.96697.78450.216
2.108-2.1940.2564300.21380470.21585640.9650.97698.98410.166
2.194-2.2910.2063940.16678380.16882450.9760.98499.84230.133
2.291-2.4030.1863740.13774720.13978490.9810.98999.96180.114
2.403-2.5320.1753880.1370970.13374870.9820.9999.97330.111
2.532-2.6850.1783460.1367830.13271290.9810.991000.115
2.685-2.870.1733130.13763710.13966840.9820.9891000.124
2.87-3.0990.1622960.12959530.1362530.9840.9999.9360.12
3.099-3.3940.1812910.14254710.14457650.9810.98899.9480.136
3.394-3.7920.1522450.13649850.13752350.9850.98999.90450.135
3.792-4.3740.1382330.12144320.12246650.9890.9911000.128
4.374-5.3470.1422120.13337460.13339620.9890.99199.8990.145
5.347-7.5170.2071650.16629650.16831430.9760.98499.58640.181
7.517-48.90.191900.19417630.19418580.9760.97399.73090.222
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)
10.40130.2541-0.01160.98810.22390.94430.0096-0.0235-0.02560.0261-0.01180.11630.1047-0.1830.00220.0946-0.0202-0.00990.08080.03280.04411.617-10.2758-2.4679
20.7002-0.1325-0.02450.7769-0.10310.88640.01360.0169-0.0219-0.0024-0.0092-0.09920.06660.1277-0.00450.06870.01050.00160.0532-0.02380.040228.8051-8.5455-34.3005
30.4073-0.20280.0250.7810.21180.99410.02690.0616-0.0035-0.0846-0.0243-0.0155-0.0788-0.0593-0.00270.06210.00670.00140.03490.0050.002217.304716.594-36.1305
40.5535-0.00260.17180.8168-0.16261.18760.0232-0.0437-0.04550.0310.00460.02-0.0168-0.0179-0.02780.03080.0033-0.00230.0213-0.00350.007319.203116.5206-0.3908
Refinement TLS group
IDRefine-IDRefine TLS-IDSelectionAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1ALLA3 - 404
2X-RAY DIFFRACTION2ALLB2 - 403
3X-RAY DIFFRACTION3ALLC3 - 404
4X-RAY DIFFRACTION4ALLD2 - 403

+
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