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- PDB-8yp6: Cryo-EM map of 30S ribosomal subunit in complex with MetAP1c of M... -
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Open data
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Basic information
Entry | Database: PDB / ID: 8yp6 | ||||||||||||||||||||||||
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Title | Cryo-EM map of 30S ribosomal subunit in complex with MetAP1c of Mycobacterium smegmatis | ||||||||||||||||||||||||
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![]() | RIBOSOME / Methionine aminopeptidase type1c / anti-association factor / inter-subunit face | ||||||||||||||||||||||||
Function / homology | ![]() methionyl aminopeptidase / initiator methionyl aminopeptidase activity / metalloaminopeptidase activity / transition metal ion binding / ribosomal small subunit biogenesis / ribosomal small subunit assembly / small ribosomal subunit / cytosolic small ribosomal subunit / small ribosomal subunit rRNA binding / tRNA binding ...methionyl aminopeptidase / initiator methionyl aminopeptidase activity / metalloaminopeptidase activity / transition metal ion binding / ribosomal small subunit biogenesis / ribosomal small subunit assembly / small ribosomal subunit / cytosolic small ribosomal subunit / small ribosomal subunit rRNA binding / tRNA binding / rRNA binding / ribosome / structural constituent of ribosome / translation / ribonucleoprotein complex / mRNA binding / proteolysis / RNA binding / zinc ion binding / cytosol / cytoplasm Similarity search - Function | ||||||||||||||||||||||||
Biological species | ![]() | ||||||||||||||||||||||||
Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 4.7 Å | ||||||||||||||||||||||||
![]() | Banerjee, A. / Srinivasan, K. / Sengupta, J. | ||||||||||||||||||||||||
Funding support | ![]()
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![]() | ![]() Title: Cryo-EM map of 30S ribosomal subunit in complex with MetAP1c of Mycobacterium smegmatis Authors: Banerjee, A. / Srinivasan, K. / Sengupta, J. | ||||||||||||||||||||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 1.1 MB | Display | ![]() |
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PDB format | ![]() | 902.8 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 39462MC M: map data used to model this data C: citing same article ( |
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Similar structure data | Similarity search - Function & homology ![]() |
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Links
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Assembly
Deposited unit | ![]()
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1 |
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Components
-RNA chain , 1 types, 1 molecules a
#1: RNA chain | Mass: 489828.562 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() References: GenBank: 118168627 |
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-Small ribosomal subunit protein ... , 17 types, 17 molecules cdefhijklnopqrtsm
#2: Protein | Mass: 23805.396 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() References: UniProt: A0QSD7 |
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#3: Protein | Mass: 23284.590 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() References: UniProt: A0QSL7 |
#4: Protein | Mass: 20443.531 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() References: UniProt: A0QSG6 |
#5: Protein | Mass: 10991.637 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() References: UniProt: A0A2U9Q0X2 |
#7: Protein | Mass: 14260.340 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() References: UniProt: A0QSG3 |
#8: Protein | Mass: 14093.392 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() References: UniProt: A0QSP9 |
#9: Protein | Mass: 11066.859 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() References: UniProt: A0QSD0 |
#10: Protein | Mass: 12380.040 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() References: UniProt: A0QSL6 |
#11: Protein | Mass: 13678.093 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() References: UniProt: A0QS96 |
#12: Protein | Mass: 6845.213 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() References: UniProt: A0QSG2 |
#13: Protein | Mass: 10079.706 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() References: UniProt: A0QVQ3 |
#14: Protein | Mass: 12635.652 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() References: UniProt: A0QV37 |
#15: Protein | Mass: 10423.152 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() References: UniProt: A0QSE0 |
#16: Protein | Mass: 7338.635 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() References: UniProt: A0R7F7 |
#17: Protein | Mass: 9353.830 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() References: UniProt: A0R102 |
#18: Protein | Mass: 9167.668 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() References: UniProt: A0QSD5 |
#20: Protein | Mass: 13445.560 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() References: UniProt: A0QSL5 |
-Protein , 2 types, 2 molecules gA
#6: Protein | Mass: 17660.375 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() References: UniProt: A0QS97 |
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#19: Protein | Mass: 32354.391 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Gene: map, MSMEI_2525 / Production host: ![]() ![]() |
-Details
Has protein modification | Y |
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-Experimental details
-Experiment
Experiment | Method: ELECTRON MICROSCOPY |
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EM experiment | Aggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction |
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Sample preparation
Component |
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Source (natural) |
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Source (recombinant) |
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Buffer solution | pH: 7.6 | ||||||||||||||||||
Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES | ||||||||||||||||||
Vitrification | Cryogen name: ETHANE |
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Electron microscopy imaging
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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Microscopy | Model: TFS KRIOS |
Electron gun | Electron source: ![]() |
Electron lens | Mode: BRIGHT FIELD / Nominal defocus max: 3300 nm / Nominal defocus min: 1800 nm |
Image recording | Electron dose: 20.7 e/Å2 / Film or detector model: FEI FALCON III (4k x 4k) |
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Processing
CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION |
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3D reconstruction | Resolution: 4.7 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 50296 / Symmetry type: POINT |