Download MendeleyActive site mutants of a fungal KDNase
Yeung, J.Y., Telford, J.C., S Shidmoossavee, F., Bennet, A.J., Taylor, G.L., Moore, M.M.To be published.
4M4V
Structural evaluation R171L mutant of the aspergillus fumigatus kdnase (sialidase)
- PDB DOI: https://doi.org/10.2210/pdb4M4V/pdb
- Classification: HYDROLASE
- Organism(s): Aspergillus fumigatus Af293
- Expression System: Escherichia coli
- Mutation(s): Yes
- Deposited: 2013-08-07 Released: 2014-09-17
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 1.84 Å
- R-Value Free: 0.194
- R-Value Work: 0.154
- R-Value Observed: 0.156
Starting Model: experimental
View more details
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 |
| Extracellular sialidase/neuraminidase, putative | 422 | Aspergillus fumigatus Af293 | Mutation(s): 1 Gene Names: AFUA_4G13800 EC: 3.2.1.18 |  | |
UniProt | |||||
Find proteins for Q4WQS0 (Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293)) Explore Q4WQS0 Go to UniProtKB: Q4WQS0 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | Q4WQS0 | ||||
Sequence AnnotationsExpand | |||||
| |||||
Small Molecules
| Ligands 4 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
| DAN Query on DAN | C [auth A] | 2-DEOXY-2,3-DEHYDRO-N-ACETYL-NEURAMINIC ACID C11 H17 N O8 JINJZWSZQKHCIP-UFGQHTETSA-N |  | ||
| GOL Query on GOL | D [auth A], H [auth A], I [auth B] | GLYCEROL C3 H8 O3 PEDCQBHIVMGVHV-UHFFFAOYSA-N |  | ||
| NO3 Query on NO3 | E [auth A], F [auth A], J [auth B], K [auth B] | NITRATE ION N O3 NHNBFGGVMKEFGY-UHFFFAOYSA-N |  | ||
| NA Query on NA | G [auth A] | SODIUM ION Na FKNQFGJONOIPTF-UHFFFAOYSA-N |  | ||
Experimental Data & Validation
Experimental Data
- Method: X-RAY DIFFRACTION
- Resolution: 1.84 Å
- R-Value Free: 0.194
- R-Value Work: 0.154
- R-Value Observed: 0.156
- Space Group: P 1 21 1
Unit Cell:
| Length ( Å ) | Angle ( ˚ ) |
|---|---|
| a = 75.88 | α = 90 |
| b = 57.97 | β = 99.89 |
| c = 94.64 | γ = 90 |
| Software Name | Purpose |
|---|---|
| MOSFLM | data reduction |
| SCALA | data scaling |
| REFMAC | refinement |
| PDB_EXTRACT | data extraction |
Entry History
Deposition Data
- Released Date: 2014-09-17 Deposition Author(s): Telford, J.C., Taylor, G.L.
Revision History (Full details and data files)
- Version 1.0: 2014-09-17
Type: Initial release - Version 1.1: 2020-07-29
Type: Remediation
Reason: Carbohydrate remediation
Changes: Data collection, Database references, Derived calculations - Version 1.2: 2023-09-20
Changes: Data collection, Database references, Refinement description, Structure summary
