2XJU
X-ray structure of the N-terminal domain of the flocculin Flo5 from Saccharomyces cerevisiae with mutation S227A in complex with calcium and a1,2-mannobiose
- PDB DOI: https://doi.org/10.2210/pdb2XJU/pdb
- Classification: CELL ADHESION
- Organism(s): Saccharomyces cerevisiae S288C
- Expression System: Escherichia coli
- Mutation(s): Yes
- Deposited: 2010-07-06 Released: 2010-12-15
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 1.70 Å
- R-Value Free: 0.197
- R-Value Work: 0.164
- R-Value Observed: 0.165
wwPDB Validation 3D Report Full Report
This is version 2.0 of the entry. See complete history.
Macromolecules
Find similar proteins by:
(by identity cutoff) | 3D Structure
Entity ID: 1 | |||||
|---|---|---|---|---|---|
| Molecule | Chains | Sequence Length | Organism | Details | Image |
| FLOCCULATION PROTEIN FLO5 | 258 | Saccharomyces cerevisiae S288C | Mutation(s): 1 |  | |
UniProt | |||||
Find proteins for P38894 (Saccharomyces cerevisiae (strain ATCC 204508 / S288c)) Explore P38894 Go to UniProtKB: P38894 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | P38894 | ||||
Sequence AnnotationsExpand | |||||
| |||||
Oligosaccharides
Small Molecules
| Ligands 4 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
| GOL Query on GOL | H [auth A] | GLYCEROL C3 H8 O3 PEDCQBHIVMGVHV-UHFFFAOYSA-N |  | ||
| CA Query on CA | C [auth A], G [auth A] | CALCIUM ION Ca BHPQYMZQTOCNFJ-UHFFFAOYSA-N |  | ||
| CL Query on CL | E [auth A] | CHLORIDE ION Cl VEXZGXHMUGYJMC-UHFFFAOYSA-M |  | ||
| NA Query on NA | D [auth A], F [auth A] | SODIUM ION Na FKNQFGJONOIPTF-UHFFFAOYSA-N |  | ||
Biologically Interesting Molecules (External Reference) 1 Unique
Entity ID: 2 | |||||
|---|---|---|---|---|---|
| ID | Chains | Name | Type/Class | 2D Diagram | 3D Interactions |
| PRD_900111 Query on PRD_900111 | B | 2alpha-alpha-mannobiose | Oligosaccharide / Metabolism |  | |
Experimental Data & Validation
Experimental Data
- Method: X-RAY DIFFRACTION
- Resolution: 1.70 Å
- R-Value Free: 0.197
- R-Value Work: 0.164
- R-Value Observed: 0.165
- Space Group: P 21 21 21
Unit Cell:
| Length ( Å ) | Angle ( ˚ ) |
|---|---|
| a = 46.47 | α = 90 |
| b = 62.57 | β = 90 |
| c = 105.77 | γ = 90 |
| Software Name | Purpose |
|---|---|
| REFMAC | refinement |
| XDS | data reduction |
| XSCALE | data scaling |
| REFMAC | phasing |
Entry History
Deposition Data
- Released Date: 2010-12-15 Deposition Author(s): Veelders, M., Brueckner, S., Ott, D., Unverzagt, C., Moesch, H.-U., Essen, L.-O.
Revision History (Full details and data files)
- Version 1.0: 2010-12-15
Type: Initial release - Version 1.1: 2011-05-08
Changes: Version format compliance - Version 1.2: 2011-07-13
Changes: Version format compliance - Version 1.3: 2017-07-05
Changes: Data collection - Version 2.0: 2020-07-29
Type: Remediation
Reason: Carbohydrate remediation
Changes: Atomic model, Data collection, Derived calculations, Other, Structure summary
