Download MendeleyCrystal structure of Flavoprotein in Complex with FMN (YP_193882.1) from Lactobacillus acidophilus NCFM at 1.20 A resolution
Joint Center for Structural Genomics (JCSG)To be published.
3EDO
Crystal structure of Flavoprotein in Complex with FMN (YP_193882.1) from Lactobacillus acidophilus NCFM at 1.20 A resolution
- PDB DOI: https://doi.org/10.2210/pdb3EDO/pdb
- Classification: FLAVOPROTEIN
- Organism(s): Lactobacillus acidophilus NCFM
- Expression System: Escherichia coli
- Mutation(s): No
- Deposited: 2008-09-03 Released: 2008-09-30
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 1.20 Å
- R-Value Free: 0.160
- R-Value Work: 0.136
- R-Value Observed: 0.137
This is version 1.4 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 trp repressor binding protein | 151 | Lactobacillus acidophilus NCFM | Mutation(s): 0 Gene Names: YP_193882.1, LBA1001 |  | |
UniProt | |||||
Find proteins for Q5FKC3 (Lactobacillus acidophilus (strain ATCC 700396 / NCK56 / N2 / NCFM)) Explore Q5FKC3 Go to UniProtKB: Q5FKC3 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | Q5FKC3 | ||||
Sequence AnnotationsExpand | |||||
| |||||
Small Molecules
| Ligands 2 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
| FMN Query on FMN | C [auth A], J [auth B] | FLAVIN MONONUCLEOTIDE C17 H21 N4 O9 P FVTCRASFADXXNN-SCRDCRAPSA-N |  | ||
| EDO Query on EDO | D [auth A] E [auth A] F [auth A] G [auth A] H [auth A] | 1,2-ETHANEDIOL C2 H6 O2 LYCAIKOWRPUZTN-UHFFFAOYSA-N |  | ||
| Modified Residues 2 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Type | Formula | 2D Diagram | Parent |
| MSE Query on MSE | A, B | L-PEPTIDE LINKING | C5 H11 N O2 Se |  | MET |
| MSO Query on MSO | A, B | L-PEPTIDE LINKING | C5 H11 N O3 Se |  | MET |
Experimental Data & Validation
Experimental Data
- Method: X-RAY DIFFRACTION
- Resolution: 1.20 Å
- R-Value Free: 0.160
- R-Value Work: 0.136
- R-Value Observed: 0.137
- Space Group: P 21 21 21
- Diffraction Data: https://doi.org/10.18430/M33EDO
Unit Cell:
| Length ( Å ) | Angle ( ˚ ) |
|---|---|
| a = 44.56 | α = 90 |
| b = 52.03 | β = 90 |
| c = 156.75 | γ = 90 |
| Software Name | Purpose |
|---|---|
| REFMAC | refinement |
| PHENIX | refinement |
| SHELX | phasing |
| MolProbity | model building |
| XSCALE | data scaling |
| PDB_EXTRACT | data extraction |
| XDS | data reduction |
| SHELXD | phasing |
| autoSHARP | phasing |
Entry History
Deposition Data
- Released Date: 2008-09-30 Deposition Author(s): Joint Center for Structural Genomics (JCSG)
Revision History (Full details and data files)
- Version 1.0: 2008-09-30
Type: Initial release - Version 1.1: 2011-07-13
Changes: Version format compliance - Version 1.2: 2017-10-25
Changes: Author supporting evidence, Refinement description - Version 1.3: 2019-07-24
Changes: Data collection, Derived calculations, Refinement description - Version 1.4: 2023-02-01
Changes: Database references, Derived calculations
