[English] 日本語
Yorodumi
- PDB-9lfx: Streptococcus mutans FtsZ -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 9lfx
TitleStreptococcus mutans FtsZ
ComponentsCell division protein FtsZ
KeywordsCELL CYCLE / Cell division
Function / homology
Function and homology information


division septum assembly / FtsZ-dependent cytokinesis / cell division site / protein polymerization / GTPase activity / GTP binding / cytoplasm
Similarity search - Function
Cell division protein FtsZ / Cell division protein FtsZ, conserved site / Cell division protein FtsZ, C-terminal / FtsZ family, C-terminal domain / FtsZ protein signature 1. / Tubulin-like protein FtsZ/CetZ / Tubulin/FtsZ family, C-terminal domain / Tubulin/FtsZ-like, C-terminal domain / Tubulin/FtsZ, C-terminal / Tubulin/FtsZ, 2-layer sandwich domain ...Cell division protein FtsZ / Cell division protein FtsZ, conserved site / Cell division protein FtsZ, C-terminal / FtsZ family, C-terminal domain / FtsZ protein signature 1. / Tubulin-like protein FtsZ/CetZ / Tubulin/FtsZ family, C-terminal domain / Tubulin/FtsZ-like, C-terminal domain / Tubulin/FtsZ, C-terminal / Tubulin/FtsZ, 2-layer sandwich domain / Tubulin/FtsZ family, GTPase domain / Tubulin/FtsZ family, GTPase domain / Tubulin/FtsZ, GTPase domain / Tubulin/FtsZ, GTPase domain superfamily
Similarity search - Domain/homology
GUANOSINE-5'-TRIPHOSPHATE / Cell division protein FtsZ
Similarity search - Component
Biological speciesStreptococcus mutans serotype c (bacteria)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3.49 Å
AuthorsYuxing, C.
Funding support1items
OrganizationGrant numberCountry
Not funded
CitationJournal: To Be Published
Title: Streptococcus mutans FtsZ
Authors: Yuxing, C.
History
DepositionJan 9, 2025Deposition site: PDBJ / Processing site: PDBC
Revision 1.0Jan 14, 2026Provider: repository / Type: Initial release

-
Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

-
Assembly

Deposited unit
B: Cell division protein FtsZ
C: Cell division protein FtsZ
D: Cell division protein FtsZ
A: Cell division protein FtsZ
hetero molecules


Theoretical massNumber of molelcules
Total (without water)129,38911
Polymers127,2234
Non-polymers2,1667
Water5,170287
1
B: Cell division protein FtsZ
hetero molecules


Theoretical massNumber of molelcules
Total (without water)32,3292
Polymers31,8061
Non-polymers5231
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
2
C: Cell division protein FtsZ
hetero molecules


Theoretical massNumber of molelcules
Total (without water)32,3533
Polymers31,8061
Non-polymers5472
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
3
D: Cell division protein FtsZ
hetero molecules


Theoretical massNumber of molelcules
Total (without water)32,3533
Polymers31,8061
Non-polymers5472
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
4
A: Cell division protein FtsZ
hetero molecules


Theoretical massNumber of molelcules
Total (without water)32,3533
Polymers31,8061
Non-polymers5472
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)173.119, 173.119, 172.282
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number96
Space group name H-MP43212

-
Components

#1: Protein
Cell division protein FtsZ


Mass: 31805.840 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Streptococcus mutans serotype c (strain ATCC 700610 / UA159) (bacteria)
Gene: ftsZ, SMU_552
Production host: Escherichia coli 'BL21-Gold(DE3)pLysS AG' (bacteria)
References: UniProt: Q8DVD9
#2: Chemical
ChemComp-GTP / GUANOSINE-5'-TRIPHOSPHATE


Mass: 523.180 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C10H16N5O14P3 / Feature type: SUBJECT OF INVESTIGATION / Comment: GTP, energy-carrying molecule*YM
#3: Chemical ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: Mg
#4: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 287 / Source method: isolated from a natural source / Formula: H2O
Has ligand of interestY
Has protein modificationN

-
Experimental details

-
Experiment

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

-
Sample preparation

CrystalDensity Matthews: 5.16 Å3/Da / Density % sol: 76.15 %
Crystal growTemperature: 296 K / Method: vapor diffusion, hanging drop / pH: 6.7 / Details: PEG10000, Potassium sodium tartrate, MES

-
Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: SSRF / Beamline: BL02U1 / Wavelength: 0.9798 Å
DetectorType: DECTRIS EIGER2 S 9M / Detector: PIXEL / Date: Oct 19, 2023
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9798 Å / Relative weight: 1
ReflectionResolution: 3.49→34.56 Å / Num. obs: 30537 / % possible obs: 90.08 % / Redundancy: 9.6 % / CC1/2: 0.99 / Net I/σ(I): 10.67
Reflection shellResolution: 3.49→3.62 Å / Num. unique obs: 30537 / CC1/2: 0.99

-
Processing

Software
NameVersionClassification
PHENIX(1.19.1_4122: ???)refinement
HKL-2000data scaling
HKL-2000data reduction
PHENIXphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT / Resolution: 3.49→34.56 Å / SU ML: 0.46 / Cross valid method: FREE R-VALUE / σ(F): 1.33 / Phase error: 27.94 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2708 2012 6.59 %
Rwork0.2218 --
obs0.225 30537 90.24 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Refinement stepCycle: LAST / Resolution: 3.49→34.56 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms8760 0 131 287 9178
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0118959
X-RAY DIFFRACTIONf_angle_d1.34112166
X-RAY DIFFRACTIONf_dihedral_angle_d19.0481323
X-RAY DIFFRACTIONf_chiral_restr0.0751491
X-RAY DIFFRACTIONf_plane_restr0.0091577
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
3.49-3.580.3619830.32231066X-RAY DIFFRACTION49
3.58-3.670.3922990.32531417X-RAY DIFFRACTION64
3.67-3.780.33511260.2971658X-RAY DIFFRACTION75
3.78-3.90.36591300.26571907X-RAY DIFFRACTION86
3.9-4.040.29721410.2542085X-RAY DIFFRACTION93
4.04-4.210.29551510.23172192X-RAY DIFFRACTION98
4.21-4.40.25711530.20622222X-RAY DIFFRACTION100
4.4-4.630.21371610.18642232X-RAY DIFFRACTION100
4.63-4.920.23611570.18142250X-RAY DIFFRACTION100
4.92-5.290.28411550.21132256X-RAY DIFFRACTION100
5.3-5.830.34711630.2792250X-RAY DIFFRACTION100
5.83-6.660.27171610.21722292X-RAY DIFFRACTION100
6.66-8.370.22291610.19642289X-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)
10.08010.0704-0.10050.0634-0.09190.1390.0458-0.0003-0.04670.0720.05340.06420.0266-0.07050.0930.2784-0.1305-0.16930.14810.02940.1534.511868.862451.9666
20.0310.0327-0.02480.034-0.0260.0229-0.0298-0.0473-0.0557-0.04160.05120.05020.1207-0.0530.01390.3187-0.1304-0.10090.15940.09230.2117.560771.055958.5244
30.07870.0232-0.09980.05390.01140.16470.169-0.0623-0.0219-0.0704-0.0546-0.12310.0680.23170.01810.33240.0431-0.11360.30760.0980.501620.833777.558157.0106
40.05170.03730.06320.04640.07890.14210.0710.0564-0.01540.06740.012-0.00010.10650.08560.11590.27220.0098-0.05320.0690.07220.149913.482370.303447.9245
50.1814-0.04650.10450.37050.01650.17340.10370.0290.0025-0.1990.12480.0650.08220.15030.09570.32490.0362-0.00830.1210.01990.08814.338773.382844.4827
60.0592-0.0334-0.01010.0723-0.05950.12330.066-0.0314-0.0363-0.14570.0288-0.00540.16350.0080.05670.3447-0.1295-0.04150.09390.07850.16784.942876.310141.3081
70.0433-0.0097-0.07270.0647-0.00830.3019-0.1522-0.0626-0.090.1218-0.07860.07290.31230.063-0.02120.5567-0.0408-0.16170.18540.01140.29275.459159.293736.395
80.00040.0005-0.00030.0202-0.00120.0188-0.02740.067-0.0673-0.0085-0.05210.06850.0527-0.09580.00450.5281-0.0812-0.18310.2415-0.11060.4003-7.080767.677629.1322
90.04380.0264-0.01660.0769-0.03670.07930.03620.0676-0.0866-0.19020.081-0.03740.03470.00840.21240.5924-0.2638-0.00930.1626-0.16770.1791-1.20557.935429.121
100.0725-0.12240.03920.2729-0.02550.0541-0.0096-0.0393-0.0196-0.04680.0410.016-0.0696-0.06520.2190.45480.06370.13620.0614-0.04630.2223-5.752361.748237.8924
110.01190.02050.00490.04580.00550.00120.0552-0.02190.00930.04010.00250.00060.00740.00460.09680.97960.00920.16550.1913-0.03810.2297-0.3979119.755849.5277
120.00640.01170.0020.04090.03870.0604-0.0468-0.05730.0314-0.0139-0.03680.061-0.0139-0.0991-0.0450.8881-0.12340.24470.2419-0.22810.4197-0.5734125.698154.2756
130.1526-0.0076-0.02490.0907-0.00020.00590.0221-0.09170.0890.07420.061-0.0220.1810.1354-0.04231.5044-0.29820.02720.5575-0.21480.563112.5231132.500755.9537
14-0.00070.00320.00190.00130.0040.00620.0321-0.0158-0.02710.19250.0206-0.1186-0.02820.07090.19031.1307-0.2392-0.33370.3441-0.07420.283312.4118119.657852.6708
150.0787-0.02450.05130.1279-0.12720.167-0.0411-0.03290.19570.4794-0.1399-0.0148-0.1340.073-0.28720.7624-0.2062-0.0931-0.0580.14730.21457.0988120.279138.6408
160.1065-0.0970.21640.0871-0.18890.4287-0.07080.00320.0230.2896-0.05-0.0639-0.19060.1057-0.29110.5388-0.0345-0.11730.1105-0.00080.0826.5572103.58444.7725
170.18320.14290.09190.12240.08070.0743-0.02080.0418-0.0214-0.00920.07-0.002-00.04860.07340.27520.09970.07210.0902-0.01260.00540.41104.480229.3136
180.01110.0161-0.0050.0375-0.01060.0044-0.0054-0.0148-0.02110.12660.00410.0832-0.058-0.0033-0.03550.276-0.08560.1620.10760.00630.1122.7834100.41138.8637
190.0594-0.05810.00620.0676-0.02640.1141-0.0479-0.03390.00230.12360.0110.0197-0.13360.0153-0.40410.3930.0450.0270.06430.03240.02361.473999.047537.4103
200.47810.0395-0.08180.00820.00240.0383-0.09080.1451-0.0126-0.020.03150.0883-0.1261-0.10330.01730.52870.004-0.01850.1485-0.0070.29093.6448158.566116.8255
210.19330.0290.08790.1954-0.02320.0463-0.20480.05540.09460.0219-0.04210.0618-0.14760.1156-0.28440.449-0.0551-0.03660.19220.19970.35921.8047166.13216.8181
220.06870.0431-0.05250.0296-0.03320.042-0.02540.01640.11950.09010.01-0.006-0.06840.0727-0.0140.7037-0.2193-0.06770.27660.13590.435213.3342174.98320.2504
230.19620.10520.03370.24280.09630.0563-0.0756-0.00790.02950.18350.0242-0.1604-0.22770.04570.14530.4162-0.0402-0.01850.06380.06510.171214.6888160.84820.6495
240.01760.01250.0030.0095-0.00140.005-0.04240.0003-0.03880.11870.055-0.0169-0.04450.119-0.00030.4041-0.148-0.17010.4860.18790.463824.5965162.452316.1368
250.6995-0.2154-0.39110.31270.02230.5151-0.04390.1816-0.19340.24150.07440.26540.1739-0.2240.06070.2636-0.0776-0.07670.11230.00690.332211.0866150.873210.4722
260.0278-0.01740.0020.0502-0.00380.0016-0.0433-0.0453-0.02980.01790.02430.0638-0.06260.0041-0.12730.4915-0.0472-0.01830.10130.13070.19199.8782144.134925.7413
270.0009-0.0012-0.00490.00640.0090.0127-0.07990.0568-0.1134-0.0634-0.0197-0.00130.2262-0.0256-0.00020.35180.03970.04670.32090.0180.390212.2282135.301211.7029
280.0367-0.00110.01280.0287-0.02870.03250.0703-0.0094-0.0769-0.0657-0.0279-0.00670.01910.00980.05490.3217-0.0364-0.08550.10630.12280.37528.623136.141821.1505
29-0.0009-0.00180.00240.0022-0.00320.0014-0.0110.0024-0.0580.1235-0.10430.0438-0.028-0.05470.01740.5552-0.0815-0.23490.1531-0.11280.41572.698622.609422.3609
300.27670.0723-0.15450.04870.01860.22360.1099-0.14850.02240.202-0.0609-0.07530.01290.1061-0.07530.5171-0.0501-0.32230.1917-0.01710.53758.724525.338729.6082
310.05640.00930.05140.00220.00830.05130.07650.0133-0.0758-0.0378-0.05360.0013-0.07050.09940.09090.59970.0031-0.3840.4217-0.20410.675920.644733.610626.2918
320.0190.00810.00760.03570.04440.09520.07430.0414-0.1222-0.03830.0323-0.06950.15340.07860.06870.4858-0.0815-0.24160.1848-0.18550.5212.099430.943317.1225
330.0310.0338-0.02450.0469-0.05880.10330.0861-0.03740.04070.08510.0084-0.0205-0.10510.05840.08670.4979-0.0597-0.1340.2203-0.25060.52273.514839.005719.2908
340.0170.00480.04360.01340.02230.18610.2215-0.19240.00130.02080.0888-0.1096-0.00140.04290.380.5451-0.2779-0.15810.1355-0.12560.3831-1.718534.49816.7226
350.00390.0023-0.02040.0001-0.00930.10850.0722-0.00650.04680.0896-0.08280.0551-0.0801-0.22140.0040.5174-0.0362-0.2080.2559-0.0580.5227-17.711934.897712.4056
360.08880.09750.08240.15850.07350.0912-0.05230.11180.1412-0.0133-0.0728-0.07230.13130.0073-0.22130.4571-0.1037-0.09020.19910.16120.3599-11.745727.18017.8689
370.0642-0.069-0.05630.07770.05470.05780.02440.05530.1328-0.0183-0.0364-0.07690.0123-0.0201-0.09060.5249-0.2092-0.16610.2280.16990.2843-14.789427.71172.7031
38-0.0006-0.001-0.00450.01350.01880.01950.0456-0.11130.08570.07350.0097-0.09930.1058-0.04980.00010.4871-0.1892-0.0930.27720.04770.2771-13.12725.759715.0445
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1chain 'B' and (resid 13 through 34 )
2X-RAY DIFFRACTION2chain 'B' and (resid 35 through 61 )
3X-RAY DIFFRACTION3chain 'B' and (resid 62 through 94 )
4X-RAY DIFFRACTION4chain 'B' and (resid 95 through 113 )
5X-RAY DIFFRACTION5chain 'B' and (resid 114 through 141 )
6X-RAY DIFFRACTION6chain 'B' and (resid 142 through 203 )
7X-RAY DIFFRACTION7chain 'B' and (resid 204 through 233 )
8X-RAY DIFFRACTION8chain 'B' and (resid 234 through 254 )
9X-RAY DIFFRACTION9chain 'B' and (resid 255 through 299 )
10X-RAY DIFFRACTION10chain 'B' and (resid 300 through 316 )
11X-RAY DIFFRACTION11chain 'C' and (resid 13 through 34 )
12X-RAY DIFFRACTION12chain 'C' and (resid 35 through 61 )
13X-RAY DIFFRACTION13chain 'C' and (resid 62 through 94 )
14X-RAY DIFFRACTION14chain 'C' and (resid 95 through 125 )
15X-RAY DIFFRACTION15chain 'C' and (resid 126 through 203 )
16X-RAY DIFFRACTION16chain 'C' and (resid 204 through 233 )
17X-RAY DIFFRACTION17chain 'C' and (resid 234 through 254 )
18X-RAY DIFFRACTION18chain 'C' and (resid 255 through 272 )
19X-RAY DIFFRACTION19chain 'C' and (resid 273 through 316 )
20X-RAY DIFFRACTION20chain 'D' and (resid 13 through 34 )
21X-RAY DIFFRACTION21chain 'D' and (resid 35 through 61 )
22X-RAY DIFFRACTION22chain 'D' and (resid 62 through 94 )
23X-RAY DIFFRACTION23chain 'D' and (resid 95 through 141 )
24X-RAY DIFFRACTION24chain 'D' and (resid 142 through 158 )
25X-RAY DIFFRACTION25chain 'D' and (resid 159 through 203 )
26X-RAY DIFFRACTION26chain 'D' and (resid 204 through 233 )
27X-RAY DIFFRACTION27chain 'D' and (resid 234 through 254 )
28X-RAY DIFFRACTION28chain 'D' and (resid 255 through 316 )
29X-RAY DIFFRACTION29chain 'A' and (resid 6 through 34 )
30X-RAY DIFFRACTION30chain 'A' and (resid 35 through 61 )
31X-RAY DIFFRACTION31chain 'A' and (resid 62 through 94 )
32X-RAY DIFFRACTION32chain 'A' and (resid 95 through 125 )
33X-RAY DIFFRACTION33chain 'A' and (resid 126 through 141 )
34X-RAY DIFFRACTION34chain 'A' and (resid 142 through 233 )
35X-RAY DIFFRACTION35chain 'A' and (resid 234 through 254 )
36X-RAY DIFFRACTION36chain 'A' and (resid 255 through 272 )
37X-RAY DIFFRACTION37chain 'A' and (resid 273 through 299 )
38X-RAY DIFFRACTION38chain 'A' and (resid 300 through 316 )

+
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