Download MendeleyCrystal structure of Protein C20orf147 homolog (17391249) from Mus musculus at 1.90 A resolution
Joint Center for Structural Genomics (JCSG)To be published.
2GFH | pdb_00002gfh
Crystal structure of a n-acetylneuraminic acid phosphatase (nanp) from mus musculus at 1.90 A resolution
- PDB DOI: https://doi.org/10.2210/pdb2GFH/pdb
- Classification: HYDROLASE
- Organism(s): Mus musculus
- Expression System: Escherichia coli
- Mutation(s): No
- Deposited: 2006-03-21 Released: 2006-04-18
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 1.90 Å
- R-Value Free: 0.259 (Depositor), 0.260 (DCC)
- R-Value Work: 0.208 (Depositor), 0.220 (DCC)
- R-Value Observed: 0.210 (Depositor)
Starting Model: experimental
View more details
wwPDB Validation 3D Report Full Report
This is version 1.4 of the entry. See complete history.
Literature
To be published.
Macromolecules
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(by identity cutoff) | 3D Structure
Entity ID: 1 | |||||
|---|---|---|---|---|---|
| Molecule | Chains | Sequence Length | Organism | Details | Image |
| haloacid dehalogenase-like hydrolase domain containing 4 | 260 | Mus musculus | Mutation(s): 0 Gene Names: 17391249 EC: 3.1.3.29 |  | |
UniProt & NIH Common Fund Data Resources | |||||
Find proteins for Q9CPT3 (Mus musculus) Explore Q9CPT3 Go to UniProtKB: Q9CPT3 | |||||
IMPC: MGI:1914561 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | Q9CPT3 | ||||
Sequence AnnotationsExpand | |||||
| |||||
Small Molecules
| Ligands 4 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
| PO4 Query on PO4 | D [auth A] | PHOSPHATE ION O4 P NBIIXXVUZAFLBC-UHFFFAOYSA-K |  | ||
| EDO Query on EDO | E [auth A] | 1,2-ETHANEDIOL C2 H6 O2 LYCAIKOWRPUZTN-UHFFFAOYSA-N |  | ||
| CL Query on CL | C [auth A] | CHLORIDE ION Cl VEXZGXHMUGYJMC-UHFFFAOYSA-M |  | ||
| NA Query on NA | B [auth A] | SODIUM ION Na FKNQFGJONOIPTF-UHFFFAOYSA-N |  | ||
Experimental Data & Validation
Experimental Data
- Method: X-RAY DIFFRACTION
- Resolution: 1.90 Å
- R-Value Free: 0.259 (Depositor), 0.260 (DCC)
- R-Value Work: 0.208 (Depositor), 0.220 (DCC)
- R-Value Observed: 0.210 (Depositor)
Diffraction Data: https://doi.org/10.18430/M32GFH
Space Group: P 61 2 2
Unit Cell:
| Length ( Å ) | Angle ( ˚ ) |
|---|---|
| a = 71.259 | α = 90 |
| b = 71.259 | β = 90 |
| c = 195.632 | γ = 120 |
| Software Name | Purpose |
|---|---|
| REFMAC | refinement |
| SCALEPACK | data scaling |
| PDB_EXTRACT | data extraction |
| DENZO | data reduction |
| MOLREP | phasing |
Entry History
Deposition Data
- Released Date: 2006-04-18 Deposition Author(s): Joint Center for Structural Genomics (JCSG)
Revision History (Full details and data files)
- Version 1.0: 2006-04-18
Type: Initial release - Version 1.1: 2008-05-01
Changes: Version format compliance - Version 1.2: 2011-07-13
Changes: Advisory, Derived calculations, Version format compliance - Version 1.3: 2023-01-25
Changes: Database references, Derived calculations - Version 1.4: 2024-04-03
Changes: Data collection, Refinement description
