Download MendeleyCrystal structure of C-terminal domain of putative exported cytochrome C biogenesis-related protein from Bacteroides fragilis
Chang, C., Tesar, C., Cobb, G., Joachimiak, A.To be published.
3F9U
Crystal structure of C-terminal domain of putative exported cytochrome C biogenesis-related protein from Bacteroides fragilis
- PDB DOI: https://doi.org/10.2210/pdb3F9U/pdb
- Classification: structural genomics, unknown function
- Organism(s): Bacteroides fragilis NCTC 9343
- Expression System: Escherichia coli
- Mutation(s): No
- Deposited: 2008-11-14 Released: 2008-12-02
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 2.20 Å
- R-Value Free: 0.236
- R-Value Work: 0.181
- R-Value Observed: 0.183
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 |
| Putative exported cytochrome C biogenesis-related protein | 172 | Bacteroides fragilis NCTC 9343 | Mutation(s): 0 Gene Names: BF3033 |  | |
UniProt | |||||
Find proteins for Q5LAZ4 (Bacteroides fragilis (strain ATCC 25285 / DSM 2151 / CCUG 4856 / JCM 11019 / NCTC 9343 / Onslow)) Explore Q5LAZ4 Go to UniProtKB: Q5LAZ4 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | Q5LAZ4 | ||||
Sequence AnnotationsExpand | |||||
| |||||
Small Molecules
| Ligands 2 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
| EDO Query on EDO | E [auth A], G [auth A] | 1,2-ETHANEDIOL C2 H6 O2 LYCAIKOWRPUZTN-UHFFFAOYSA-N |  | ||
| NO3 Query on NO3 | C [auth A], D [auth A], F [auth A], H [auth A], I [auth B] | NITRATE ION N O3 NHNBFGGVMKEFGY-UHFFFAOYSA-N |  | ||
| Modified Residues 1 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Type | Formula | 2D Diagram | Parent |
| MSE Query on MSE | A, B | L-PEPTIDE LINKING | C5 H11 N O2 Se |  | MET |
Experimental Data & Validation
Experimental Data
- Method: X-RAY DIFFRACTION
- Resolution: 2.20 Å
- R-Value Free: 0.236
- R-Value Work: 0.181
- R-Value Observed: 0.183
- Space Group: P 43 21 2
Unit Cell:
| Length ( Å ) | Angle ( ˚ ) |
|---|---|
| a = 64.16 | α = 90 |
| b = 64.16 | β = 90 |
| c = 181.555 | γ = 90 |
| Software Name | Purpose |
|---|---|
| SBC-Collect | data collection |
| HKL-3000 | phasing |
| MLPHARE | phasing |
| DM | model building |
| SHELXD | phasing |
| RESOLVE | model building |
| Coot | model building |
| REFMAC | refinement |
| HKL-3000 | data reduction |
| HKL-3000 | data scaling |
| DM | phasing |
| RESOLVE | phasing |
Entry History
Deposition Data
- Released Date: 2008-12-02 Deposition Author(s): Chang, C., Tesar, C., Cobb, G., Joachimiak, A., Midwest Center for Structural Genomics (MCSG)
Revision History (Full details and data files)
- Version 1.0: 2008-12-02
Type: Initial release - Version 1.1: 2011-07-13
Changes: Advisory, Refinement description, Version format compliance - Version 1.2: 2023-12-27
Changes: Data collection, Database references, Derived calculations
