Download MendeleyComprehensive analysis of protein-protein interactions between MbtH-like protein FscK and adenylation domains in nonribosomal biosynthesis of Fuscachelins.
Bruner, S.D., Zagulyaeva, A.A.To be published.
6EBY | pdb_00006eby
Crystal structure of the MbtH-like protein FscK bound to the interface forming region of FscH adenylation domain from Thermobifida fusca
- PDB DOI: https://doi.org/10.2210/pdb6EBY/pdb
- Classification: PROTEIN BINDING
- Organism(s): Thermobifida fusca YX
- Expression System: Escherichia coli BL21(DE3)
- Mutation(s): No
- Deposited: 2018-08-07 Released: 2019-08-21
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 1.85 Å
- R-Value Free: 0.235 (Depositor), 0.240 (DCC)
- R-Value Work: 0.200 (Depositor), 0.200 (DCC)
- R-Value Observed: 0.203 (Depositor)
Starting Model: experimental
View more details
wwPDB Validation 3D Report Full Report
This is version 1.2 of the entry. See complete history.
Literature
To be published.
Macromolecules
Find similar proteins by:
(by identity cutoff) | 3D Structure
Entity ID: 1 | |||||
|---|---|---|---|---|---|
| Molecule | Chains | Sequence Length | Organism | Details | Image |
| Conserved protein MbtH | 81 | Thermobifida fusca YX | Mutation(s): 0 Gene Names: Tfu_1863 |  | |
UniProt | |||||
Find proteins for Q47NS3 (Thermobifida fusca (strain YX)) Explore Q47NS3 Go to UniProtKB: Q47NS3 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | Q47NS3 | ||||
Sequence AnnotationsExpand | |||||
| |||||
Find similar proteins by:
(by identity cutoff) | 3D Structure
Entity ID: 2 | |||||
|---|---|---|---|---|---|
| Molecule | Chains | Sequence Length | Organism | Details | Image |
| Amino acid adenylation | 77 | Thermobifida fusca YX | Mutation(s): 0 Gene Names: Tfu_1866 |  | |
UniProt | |||||
Find proteins for Q47NS0 (Thermobifida fusca (strain YX)) Explore Q47NS0 Go to UniProtKB: Q47NS0 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | Q47NS0 | ||||
Sequence AnnotationsExpand | |||||
| |||||
Experimental Data & Validation
Experimental Data
- Method: X-RAY DIFFRACTION
- Resolution: 1.85 Å
- R-Value Free: 0.235 (Depositor), 0.240 (DCC)
- R-Value Work: 0.200 (Depositor), 0.200 (DCC)
- R-Value Observed: 0.203 (Depositor)
Space Group: P 1 21 1
Unit Cell:
| Length ( Å ) | Angle ( ˚ ) |
|---|---|
| a = 43.45 | α = 90 |
| b = 58.29 | β = 107.21 |
| c = 58.7 | γ = 90 |
| Software Name | Purpose |
|---|---|
| PHENIX | refinement |
| MOSFLM | data reduction |
| SCALA | data scaling |
| PHASER | phasing |
Entry History
Deposition Data
- Released Date: 2019-08-21 Deposition Author(s): Bruner, S.D., Zagulyaeva, A.A.
Revision History (Full details and data files)
- Version 1.0: 2019-08-21
Type: Initial release - Version 1.1: 2020-01-29
Changes: Derived calculations - Version 1.2: 2023-10-11
Changes: Data collection, Database references, Refinement description
