Download MendeleyCrystal structure of novel predicted phosphatase from Haemophilus somnus 129PT at 1.90 A resolution
Joint Center for Structural Genomics (JCSG)To be published.
2HSZ | pdb_00002hsz
Crystal structure of a predicted phosphoglycolate phosphatase (hs_0176) from haemophilus somnus 129pt at 1.90 A resolution
- PDB DOI: https://doi.org/10.2210/pdb2HSZ/pdb
- Classification: HYDROLASE
- Organism(s): Histophilus somni 129PT
- Expression System: Escherichia coli
- Mutation(s): No
- Deposited: 2006-07-24 Released: 2006-08-15
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 1.90 Å
- R-Value Free: 0.205 (Depositor), 0.211 (DCC)
- R-Value Work: 0.169 (Depositor), 0.175 (DCC)
- R-Value Observed: 0.171 (Depositor)
wwPDB Validation 3D Report Full Report
This is version 1.5 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 |
| novel predicted phosphatase | 243 | Histophilus somni 129PT | Mutation(s): 0 EC: 3.1.3.18 |  | |
UniProt | |||||
Find proteins for Q0I1W8 (Histophilus somni (strain 129Pt)) Explore Q0I1W8 Go to UniProtKB: Q0I1W8 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | Q0I1W8 | ||||
Sequence AnnotationsExpand | |||||
| |||||
Small Molecules
| Ligands 3 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
| ACT Query on ACT | C [auth A], F [auth B] | ACETATE ION C2 H3 O2 QTBSBXVTEAMEQO-UHFFFAOYSA-M |  | ||
| CL Query on CL | D [auth A], G [auth B] | CHLORIDE ION Cl VEXZGXHMUGYJMC-UHFFFAOYSA-M |  | ||
| UNL Query on UNL | E [auth A], H [auth B] | Unknown ligand VEXZGXHMUGYJMC-UHFFFAOYSA-M | |||
| 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: 1.90 Å
- R-Value Free: 0.205 (Depositor), 0.211 (DCC)
- R-Value Work: 0.169 (Depositor), 0.175 (DCC)
- R-Value Observed: 0.171 (Depositor)
Diffraction Data: https://doi.org/10.18430/M32HSZ
Space Group: P 21 21 2
Unit Cell:
| Length ( Å ) | Angle ( ˚ ) |
|---|---|
| a = 81.617 | α = 90 |
| b = 118.436 | β = 90 |
| c = 66.503 | γ = 90 |
| Software Name | Purpose |
|---|---|
| MolProbity | model building |
| SHELX | phasing |
| REFMAC | refinement |
| SCALA | data scaling |
| PDB_EXTRACT | data extraction |
| MOSFLM | data reduction |
| CCP4 | data scaling |
| autoSHARP | phasing |
Entry History
Deposition Data
- Released Date: 2006-08-15 Deposition Author(s): Joint Center for Structural Genomics (JCSG)
Revision History (Full details and data files)
- Version 1.0: 2006-08-15
Type: Initial release - Version 1.1: 2008-05-01
Changes: Version format compliance - Version 1.2: 2011-07-13
Changes: Advisory, Version format compliance - Version 1.3: 2017-10-18
Changes: Refinement description - Version 1.4: 2017-10-25
Changes: Author supporting evidence - Version 1.5: 2024-11-20
Changes: Data collection, Database references, Derived calculations, Refinement description, Structure summary
