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- PDB-4adv: Structure of the E. coli methyltransferase KsgA bound to the E. c... -

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Entry
Database: PDB / ID: 4adv
TitleStructure of the E. coli methyltransferase KsgA bound to the E. coli 30S ribosomal subunit
Components
  • (30S RIBOSOMAL PROTEIN ...) x 20
  • 16S RIBOSOMAL RNA
  • RIBOSOMAL RNA SMALL SUBUNIT METHYLTRANSFERASE A
KeywordsTRANSLATION / RIBOSOME BIOGENESIS / SMALL RIBOSOMAL SUBUNIT
Function / homology
Function and homology information


16S rRNA (adenine1518-N6/adenine1519-N6)-dimethyltransferase / 16S rRNA (adenine(1518)-N(6)/adenine(1519)-N(6))-dimethyltransferase activity / rRNA (adenine-N6,N6-)-dimethyltransferase activity / rRNA base methylation / rRNA methylation / ornithine decarboxylase inhibitor activity / transcription antitermination factor activity, RNA binding / ribosomal small subunit binding / misfolded RNA binding / Group I intron splicing ...16S rRNA (adenine1518-N6/adenine1519-N6)-dimethyltransferase / 16S rRNA (adenine(1518)-N(6)/adenine(1519)-N(6))-dimethyltransferase activity / rRNA (adenine-N6,N6-)-dimethyltransferase activity / rRNA base methylation / rRNA methylation / ornithine decarboxylase inhibitor activity / transcription antitermination factor activity, RNA binding / ribosomal small subunit binding / misfolded RNA binding / Group I intron splicing / RNA folding / four-way junction DNA binding / negative regulation of translational initiation / regulation of mRNA stability / mRNA regulatory element binding translation repressor activity / positive regulation of RNA splicing / regulation of DNA-templated transcription elongation / transcription elongation factor complex / DNA endonuclease activity / transcription antitermination / maturation of SSU-rRNA / DNA-templated transcription termination / maintenance of translational fidelity / mRNA 5'-UTR binding / rRNA processing / ribosome biogenesis / regulation of translation / ribosomal small subunit biogenesis / ribosomal small subunit assembly / small ribosomal subunit / small ribosomal subunit rRNA binding / double-stranded DNA binding / cytosolic small ribosomal subunit / cytoplasmic translation / tRNA binding / negative regulation of translation / rRNA binding / structural constituent of ribosome / ribosome / translation / response to antibiotic / mRNA binding / RNA binding / zinc ion binding / membrane / cytoplasm / cytosol
Similarity search - Function
rRNA adenine dimethylase-like, C-terminal / Ribosomal RNA adenine dimethylase / Ribosomal RNA adenine methylase transferase, conserved site / Ribosomal RNA adenine dimethylases signature. / Ribosomal RNA adenine methylase transferase, N-terminal / Ribosomal RNA adenine dimethylases / Ribosomal RNA adenine methyltransferase KsgA/Erm / Ribosomal RNA adenine dimethylase / rRNA adenine N(6)-methyltransferase family profile. / Ribosomal protein S21, conserved site ...rRNA adenine dimethylase-like, C-terminal / Ribosomal RNA adenine dimethylase / Ribosomal RNA adenine methylase transferase, conserved site / Ribosomal RNA adenine dimethylases signature. / Ribosomal RNA adenine methylase transferase, N-terminal / Ribosomal RNA adenine dimethylases / Ribosomal RNA adenine methyltransferase KsgA/Erm / Ribosomal RNA adenine dimethylase / rRNA adenine N(6)-methyltransferase family profile. / Ribosomal protein S21, conserved site / Ribosomal protein S21 signature. / Ribosomal protein S14, bacterial/plastid / Ribosomal protein S21 superfamily / Ribosomal protein S21 / Ribosomal protein S16, conserved site / Ribosomal protein S16 signature. / Ribosomal protein S21 / Ribosomal protein S3, bacterial-type / Ribosomal protein S19, bacterial-type / Ribosomal protein S13, bacterial-type / Ribosomal protein S6, conserved site / Ribosomal protein S6 signature. / Ribosomal protein S7, bacterial/organellar-type / Ribosomal protein S11, bacterial-type / Ribosomal protein S20 / Ribosomal protein S20 superfamily / Ribosomal protein S20 / Ribosomal protein S4, bacterial-type / 30S ribosomal protein S17 / Ribosomal protein S5, bacterial-type / Ribosomal protein S6, plastid/chloroplast / Ribosomal protein S2, bacteria/mitochondria/plastid / Ribosomal protein S9, bacterial/plastid / Ribosomal protein S18, conserved site / Ribosomal protein S18 signature. / Ribosomal protein S16 / Ribosomal protein S16 domain superfamily / Ribosomal protein S16 / Ribosomal protein S15, bacterial-type / Ribosomal protein S6 / Ribosomal protein S6 / Ribosomal protein S6 superfamily / Ribosomal protein S12, bacterial-type / Translation elongation factor EF1B/ribosomal protein S6 / Ribosomal protein S18 / Ribosomal protein S18 / Ribosomal protein S18 superfamily / K Homology domain / K homology RNA-binding domain / Ribosomal protein S2 signature 2. / Ribosomal protein S3, conserved site / Ribosomal protein S3 signature. / Ribosomal protein S10, conserved site / Ribosomal protein S10 signature. / Ribosomal protein S14, conserved site / Ribosomal protein S14 signature. / Ribosomal protein S2 signature 1. / KH domain / Type-2 KH domain profile. / K Homology domain, type 2 / Ribosomal protein S3, C-terminal / Ribosomal protein S3, C-terminal domain / Ribosomal protein S3, C-terminal domain superfamily / Ribosomal protein S15/S19, conserved site / Ribosomal protein S19 signature. / Ribosomal protein S10 / Ribosomal protein S5, N-terminal, conserved site / Ribosomal protein S5 signature. / Ribosomal protein S19/S15 / Ribosomal protein S19/S15, superfamily / Ribosomal protein S19 / Ribosomal protein S2, conserved site / Ribosomal protein S2 / Ribosomal protein S2, flavodoxin-like domain superfamily / Ribosomal protein S2 / Ribosomal protein S7, conserved site / Ribosomal protein S7 signature. / : / K homology domain superfamily, prokaryotic type / Ribosomal protein S5 / S5 double stranded RNA-binding domain profile. / Ribosomal protein S5, N-terminal / Ribosomal protein S5, C-terminal / Ribosomal protein S5, N-terminal domain / Ribosomal protein S5, C-terminal domain / Ribosomal protein S17, conserved site / Ribosomal protein S17 signature. / Ribosomal protein S13, conserved site / Ribosomal protein S13 signature. / Ribosomal protein S13 / 30s ribosomal protein S13, C-terminal / Ribosomal protein S13/S18 / Ribosomal protein S13 family profile. / Ribosomal protein S8 signature. / Ribosomal protein S14 / Ribosomal protein S14p/S29e / Ribosomal protein S4/S9 N-terminal domain / Ribosomal protein S4, conserved site / Ribosomal protein S15 signature. / Ribosomal protein S4 signature.
Similarity search - Domain/homology
: / RNA / RNA (> 10) / RNA (> 100) / RNA (> 1000) / Small ribosomal subunit protein bS6 / Small ribosomal subunit protein uS7 / 30S ribosomal protein S14 / 30S ribosomal protein S15 / 30S ribosomal protein S17 ...: / RNA / RNA (> 10) / RNA (> 100) / RNA (> 1000) / Small ribosomal subunit protein bS6 / Small ribosomal subunit protein uS7 / 30S ribosomal protein S14 / 30S ribosomal protein S15 / 30S ribosomal protein S17 / Ribosomal RNA small subunit methyltransferase A / Small ribosomal subunit protein uS10 / Small ribosomal subunit protein uS11 / Small ribosomal subunit protein uS12 / Small ribosomal subunit protein uS13 / Small ribosomal subunit protein bS16 / Small ribosomal subunit protein bS18 / Small ribosomal subunit protein uS19 / Small ribosomal subunit protein bS20 / Small ribosomal subunit protein uS2 / Small ribosomal subunit protein uS3 / Small ribosomal subunit protein uS4 / Small ribosomal subunit protein uS5 / Small ribosomal subunit protein uS8 / Small ribosomal subunit protein uS9 / Small ribosomal subunit protein uS15 / Small ribosomal subunit protein uS14 / Small ribosomal subunit protein uS17 / Small ribosomal subunit protein bS21
Similarity search - Component
Biological speciesESCHERICHIA COLI (E. coli)
MethodELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 13.5 Å
AuthorsBoehringer, D. / O'Farrell, H.C. / Rife, J.P. / Ban, N.
CitationJournal: J Biol Chem / Year: 2012
Title: Structural insights into methyltransferase KsgA function in 30S ribosomal subunit biogenesis.
Authors: Daniel Boehringer / Heather C O'Farrell / Jason P Rife / Nenad Ban /
Abstract: The assembly of the ribosomal subunits is facilitated by ribosome biogenesis factors. The universally conserved methyltransferase KsgA modifies two adjacent adenosine residues in the 3'-terminal ...The assembly of the ribosomal subunits is facilitated by ribosome biogenesis factors. The universally conserved methyltransferase KsgA modifies two adjacent adenosine residues in the 3'-terminal helix 45 of the 16 S ribosomal RNA (rRNA). KsgA recognizes its substrate adenosine residues only in the context of a near mature 30S subunit and is required for the efficient processing of the rRNA termini during ribosome biogenesis. Here, we present the cryo-EM structure of KsgA bound to a nonmethylated 30S ribosomal subunit. The structure reveals that KsgA binds to the 30S platform with the catalytic N-terminal domain interacting with substrate adenosine residues in helix 45 and the C-terminal domain making extensive contacts to helix 27 and helix 24. KsgA excludes the penultimate rRNA helix 44 from adopting its position in the mature 30S subunit, blocking the formation of the decoding site and subunit joining. We suggest that the activation of methyltransferase activity and subsequent dissociation of KsgA control conformational changes in helix 44 required for final rRNA processing and translation initiation.
History
DepositionJan 3, 2012Deposition site: PDBE / Processing site: PDBE
Revision 1.0Feb 15, 2012Provider: repository / Type: Initial release
Revision 1.1Apr 4, 2012Group: Other
Revision 1.2Sep 25, 2013Group: Other
Revision 1.3Aug 23, 2017Group: Data collection / Derived calculations ...Data collection / Derived calculations / Refinement description / Structure summary
Category: em_3d_fitting / em_image_scans ...em_3d_fitting / em_image_scans / em_software / entity / struct_conn
Item: _em_3d_fitting.target_criteria / _em_software.fitting_id ..._em_3d_fitting.target_criteria / _em_software.fitting_id / _em_software.image_processing_id / _entity.src_method
Revision 1.4Apr 4, 2018Group: Data collection / Database references / Category: citation / Item: _citation.page_last
Revision 1.5Apr 11, 2018Group: Data collection / Source and taxonomy / Category: entity_src_nat
Revision 1.6May 8, 2024Group: Data collection / Database references / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / em_3d_fitting_list / pdbx_initial_refinement_model
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _em_3d_fitting_list.accession_code / _em_3d_fitting_list.initial_refinement_model_id / _em_3d_fitting_list.source_name / _em_3d_fitting_list.type

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Structure visualization

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Assembly

Deposited unit
A: 16S RIBOSOMAL RNA
B: 30S RIBOSOMAL PROTEIN S2
C: 30S RIBOSOMAL PROTEIN S3
D: 30S RIBOSOMAL PROTEIN S4
E: 30S RIBOSOMAL PROTEIN S5
F: 30S RIBOSOMAL PROTEIN S6
G: 30S RIBOSOMAL PROTEIN S7
H: 30S RIBOSOMAL PROTEIN S8
I: 30S RIBOSOMAL PROTEIN S9
J: 30S RIBOSOMAL PROTEIN S10
K: 30S RIBOSOMAL PROTEIN S11
L: 30S RIBOSOMAL PROTEIN S12
M: 30S RIBOSOMAL PROTEIN S13
N: 30S RIBOSOMAL PROTEIN S14
O: 30S RIBOSOMAL PROTEIN S15
P: 30S RIBOSOMAL PROTEIN S16
Q: 30S RIBOSOMAL PROTEIN S17
R: 30S RIBOSOMAL PROTEIN S18
S: 30S RIBOSOMAL PROTEIN S19
T: 30S RIBOSOMAL PROTEIN S20
U: 30S RIBOSOMAL PROTEIN S21
V: RIBOSOMAL RNA SMALL SUBUNIT METHYLTRANSFERASE A


Theoretical massNumber of molelcules
Total (without water)815,55722
Polymers815,55722
Non-polymers00
Water2,504139
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1

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Components

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30S RIBOSOMAL PROTEIN ... , 20 types, 20 molecules BCDEFGHIJKLMNOPQRSTU

#2: Protein 30S RIBOSOMAL PROTEIN S2


Mass: 26650.475 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ESCHERICHIA COLI (E. coli) / Variant: KASUGAMYCIN RESISTANT / Strain: MRE600 / References: UniProt: P0A7V0
#3: Protein 30S RIBOSOMAL PROTEIN S3


Mass: 25900.117 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ESCHERICHIA COLI (E. coli) / Variant: KASUGAMYCIN RESISTANT / Strain: MRE600 / References: UniProt: P0A7V3
#4: Protein 30S RIBOSOMAL PROTEIN S4


Mass: 23383.002 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ESCHERICHIA COLI (E. coli) / Variant: KASUGAMYCIN RESISTANT / Strain: MRE600 / References: UniProt: P0A7V8
#5: Protein 30S RIBOSOMAL PROTEIN S5


Mass: 17498.203 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ESCHERICHIA COLI (E. coli) / Variant: KASUGAMYCIN RESISTANT / Strain: MRE600 / References: UniProt: P0A7W1
#6: Protein 30S RIBOSOMAL PROTEIN S6


Mass: 15727.512 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ESCHERICHIA COLI (E. coli) / Variant: KASUGAMYCIN RESISTANT / Strain: MRE600 / References: UniProt: P02358
#7: Protein 30S RIBOSOMAL PROTEIN S7


Mass: 19923.959 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ESCHERICHIA COLI (E. coli) / Variant: KASUGAMYCIN RESISTANT / Strain: MRE600 / References: UniProt: P02359
#8: Protein 30S RIBOSOMAL PROTEIN S8


Mass: 14015.361 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ESCHERICHIA COLI (E. coli) / Variant: KASUGAMYCIN RESISTANT / Strain: MRE600 / References: UniProt: P0A7W7
#9: Protein 30S RIBOSOMAL PROTEIN S9


Mass: 14755.074 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ESCHERICHIA COLI (E. coli) / Variant: KASUGAMYCIN RESISTANT / Strain: MRE600 / References: UniProt: P0A7X3
#10: Protein 30S RIBOSOMAL PROTEIN S10


Mass: 11755.597 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ESCHERICHIA COLI (E. coli) / Variant: KASUGAMYCIN RESISTANT / Strain: MRE600 / References: UniProt: P0A7R5
#11: Protein 30S RIBOSOMAL PROTEIN S11


Mass: 13739.778 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ESCHERICHIA COLI (E. coli) / Variant: KASUGAMYCIN RESISTANT / Strain: MRE600 / References: UniProt: P0A7R9
#12: Protein 30S RIBOSOMAL PROTEIN S12


Mass: 13636.961 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ESCHERICHIA COLI (E. coli) / Variant: KASUGAMYCIN RESISTANT / Strain: MRE600 / References: UniProt: P0A7S3
#13: Protein 30S RIBOSOMAL PROTEIN S13


Mass: 12997.271 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ESCHERICHIA COLI (E. coli) / Variant: KASUGAMYCIN RESISTANT / Strain: MRE600 / References: UniProt: P0A7S9
#14: Protein 30S RIBOSOMAL PROTEIN S14


Mass: 11475.364 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ESCHERICHIA COLI (E. coli) / Variant: KASUGAMYCIN RESISTANT / Strain: MRE600 / References: UniProt: P02370, UniProt: P0AG59*PLUS
#15: Protein 30S RIBOSOMAL PROTEIN S15


Mass: 10319.882 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ESCHERICHIA COLI (E. coli) / Variant: KASUGAMYCIN RESISTANT / Strain: MRE600 / References: UniProt: P02371, UniProt: P0ADZ4*PLUS
#16: Protein 30S RIBOSOMAL PROTEIN S16


Mass: 9207.572 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ESCHERICHIA COLI (E. coli) / Variant: KASUGAMYCIN RESISTANT / Strain: MRE600 / References: UniProt: P0A7T3
#17: Protein 30S RIBOSOMAL PROTEIN S17


Mass: 9593.296 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ESCHERICHIA COLI (E. coli) / Variant: KASUGAMYCIN RESISTANT / Strain: MRE600 / References: UniProt: P02373, UniProt: P0AG63*PLUS
#18: Protein 30S RIBOSOMAL PROTEIN S18


Mass: 8874.276 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ESCHERICHIA COLI (E. coli) / Variant: KASUGAMYCIN RESISTANT / Strain: MRE600 / References: UniProt: P0A7T7
#19: Protein 30S RIBOSOMAL PROTEIN S19


Mass: 10324.160 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ESCHERICHIA COLI (E. coli) / Variant: KASUGAMYCIN RESISTANT / Strain: MRE600 / References: UniProt: P0A7U3
#20: Protein 30S RIBOSOMAL PROTEIN S20


Mass: 9577.268 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ESCHERICHIA COLI (E. coli) / Variant: KASUGAMYCIN RESISTANT / Strain: MRE600 / References: UniProt: P0A7U7
#21: Protein 30S RIBOSOMAL PROTEIN S21


Mass: 8524.039 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ESCHERICHIA COLI (E. coli) / Variant: KASUGAMYCIN RESISTANT / Strain: MRE600 / References: UniProt: P68679

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RNA chain / Protein / Non-polymers , 3 types, 141 molecules AV

#1: RNA chain 16S RIBOSOMAL RNA


Mass: 499690.031 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ESCHERICHIA COLI (E. coli) / Variant: KASUGAMYCIN RESISTANT / Strain: MRE600 / References: GenBank: 33357879
#22: Protein RIBOSOMAL RNA SMALL SUBUNIT METHYLTRANSFERASE A / 16S RRNA (ADENINE(1518)-N(6)/ADENINE(1519)-N(6))-DIMETHYLTRANSFERASE / 16S RRNA DIMETHYLADENOSINE ...16S RRNA (ADENINE(1518)-N(6)/ADENINE(1519)-N(6))-DIMETHYLTRANSFERASE / 16S RRNA DIMETHYLADENOSINE TRANSFERASE / 16S RRNA DIMETHYLASE / HIGH LEVEL KASUGAMYCIN RESISTANCE PROTEIN KSGA / KASUGAMYCIN DIMETHYLTRANSFERASE / S-ADENOSYLMETHIONINE-6-N\ / N'-ADENOSYL(RRNA) DIMETHYLTRANSFERASE / METHYLTRANSFERASE KSGA


Mass: 27988.273 Da / Num. of mol.: 1 / Fragment: RESIDUES 17-268
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) ESCHERICHIA COLI (E. coli) / Plasmid: PET15B / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): K-12 / Variant (production host): HMS174
References: UniProt: P06992, 16S rRNA (adenine1518-N6/adenine1519-N6)-dimethyltransferase
#23: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 139 / Source method: isolated from a natural source / Formula: H2O

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Experimental details

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Experiment

ExperimentMethod: ELECTRON MICROSCOPY
EM experimentAggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction

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Sample preparation

ComponentName: E. COLI METHYLTRANSFERASE KSGA BOUND TO THE E. COLI 30S RIBOSOMAL SUBUNIT
Type: COMPLEX
Buffer solutionName: 40 MM KCL, 4MM MGCL2, 20 MM HEPES/KOH PH 7. 6, 6 MM 2- MERCAPTOETHANOL
pH: 7.6
Details: 40 MM KCL, 4MM MGCL2, 20 MM HEPES/KOH PH 7. 6, 6 MM 2- MERCAPTOETHANOL
SpecimenEmbedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES
Specimen supportDetails: HOLEY CARBON
VitrificationInstrument: HOMEMADE PLUNGER / Cryogen name: ETHANE
Details: VITRIFICATION 1 -- CRYOGEN- ETHANE, INSTRUMENT- PLUNGER,

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Electron microscopy imaging

MicroscopyModel: FEI TECNAI 20
Details: SEMI-AUTOMATIC DATA ACQUISITION WITH SERIAL EM SCRIPT
Electron gunElectron source: FIELD EMISSION GUN / Accelerating voltage: 200 kV / Illumination mode: SPOT SCAN
Electron lensMode: BRIGHT FIELD / Nominal magnification: 62000 X / Calibrated magnification: 82000 X / Nominal defocus max: 4000 nm / Nominal defocus min: 2000 nm
Image recordingElectron dose: 20 e/Å2 / Film or detector model: GATAN ULTRASCAN 4000 (4k x 4k)
Radiation wavelengthRelative weight: 1

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Processing

EM software
IDNameVersionCategory
1UCSF Chimeramodel fitting
2IMAGIC53D reconstruction
3SPIDER3D reconstruction
CTF correctionDetails: PER IMAGE, CTFFIND3
SymmetryPoint symmetry: C1 (asymmetric)
3D reconstructionMethod: ANGULAR RECONSTITUTION, PROJECTION MATCHING / Resolution: 13.5 Å / Num. of particles: 23343 / Actual pixel size: 3.07 Å
Details: 30S RIBOSOMAL SUBUNIT HEAD AND BODY WERE FITTED SEPARATELY AS RIGID BODIES. SUBMISSION BASED ON EXPERIMENTAL DATA FROM EMDB EMD-2017. (DEPOSITION ID: 10519).
Symmetry type: POINT
Atomic model buildingProtocol: RIGID BODY FIT / Space: REAL / Target criteria: Cross-correlation coefficient / Details: METHOD--RIGID BODY REFINEMENT PROTOCOL--XRAY
Atomic model building
IDPDB-ID 3D fitting-IDAccession codeInitial refinement model-IDSource nameType
12AVY

2avy
PDB Unreleased entry

12AVY1PDBexperimental model
21QYR

1qyr

11QYR2PDBexperimental model
RefinementHighest resolution: 13.5 Å
Refinement stepCycle: LAST / Highest resolution: 13.5 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms20487 30262 0 139 50888

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