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Open data
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Basic information
| Entry | Database: PDB / ID: 8kic | ||||||||||||||||||||||||
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| Title | Bacterial serine protease | ||||||||||||||||||||||||
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Keywords | HYDROLASE / Seine protease | ||||||||||||||||||||||||
| Function / homology | Function and homology information | ||||||||||||||||||||||||
| Biological species | ![]() ![]() | ||||||||||||||||||||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 2.5 Å | ||||||||||||||||||||||||
Authors | Lee, I.-G. / Jeon, H. | ||||||||||||||||||||||||
| Funding support | Korea, Republic Of, 1items
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Citation | Journal: To Be PublishedTitle: Structure of bacterial serine protease Authors: Lee, I.-G. / Jeon, H. | ||||||||||||||||||||||||
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Structure visualization
| Structure viewer | Molecule: Molmil Jmol/JSmol |
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Downloads & links
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Download
| PDBx/mmCIF format | 8kic.cif.gz | 233.4 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb8kic.ent.gz | 177 KB | Display | PDB format |
| PDBx/mmJSON format | 8kic.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 8kic_validation.pdf.gz | 1.3 MB | Display | wwPDB validaton report |
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| Full document | 8kic_full_validation.pdf.gz | 1.3 MB | Display | |
| Data in XML | 8kic_validation.xml.gz | 47.6 KB | Display | |
| Data in CIF | 8kic_validation.cif.gz | 71.5 KB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ki/8kic ftp://data.pdbj.org/pub/pdb/validation_reports/ki/8kic | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 37257MC M: map data used to model this data C: citing same article ( |
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| Similar structure data | Similarity search - Function & homology F&H Search |
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Links
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Assembly
| Deposited unit | ![]()
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Components
| #1: Protein | Mass: 48361.047 Da / Num. of mol.: 6 / Mutation: S214A Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() #2: Protein/peptide | | Mass: 698.854 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() #3: Protein/peptide | | Mass: 443.539 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() #4: Protein/peptide | | Mass: 613.749 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() Has protein modification | N | |
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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 | Name: Bacterial serine protease-lysozyme complex / Type: COMPLEX / Entity ID: all / Source: RECOMBINANT |
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| Source (natural) | Organism: ![]() |
| Source (recombinant) | Organism: ![]() |
| Buffer solution | pH: 7.5 |
| 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: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM |
| Electron lens | Mode: BRIGHT FIELD / Nominal defocus max: 1700 nm / Nominal defocus min: 700 nm |
| Image recording | Electron dose: 67.7 e/Å2 / Film or detector model: GATAN K3 BIOQUANTUM (6k x 4k) |
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Processing
| EM software | Name: PHENIX / Category: model refinement | ||||||||||||||||||||||||
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| CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||||||||||||||
| 3D reconstruction | Resolution: 2.5 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 382427 / Symmetry type: POINT | ||||||||||||||||||||||||
| Refine LS restraints |
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About Yorodumi







Korea, Republic Of, 1items
Citation

PDBj

FIELD EMISSION GUN