Download MendeleyThe Structure of Putative Phosphohistidine Phosphatase SixA from Nakamurella multipartitia.
Cuff, M.E., Holowicki, J., Endres, M., Joachimiak, A.To be published.
4HBZ
The Structure of Putative Phosphohistidine Phosphatase SixA from Nakamurella multipartitia.
- PDB DOI: https://doi.org/10.2210/pdb4HBZ/pdb
- Classification: HYDROLASE, ISOMERASE
- Organism(s): Nakamurella multipartita DSM 44233
- Expression System: Escherichia coli BL21(DE3)
- Mutation(s): No
- Deposited: 2012-09-28 Released: 2012-10-17
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 1.55 Å
- R-Value Free: 0.161
- R-Value Work: 0.141
- R-Value Observed: 0.142
wwPDB Validation 3D Report Full Report
This is version 1.1 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 phosphohistidine phosphatase, SixA | 186 | Nakamurella multipartita DSM 44233 | Mutation(s): 0 Gene Names: Namu_4970 |  | |
UniProt | |||||
Find proteins for C8XA43 (Nakamurella multipartita (strain ATCC 700099 / DSM 44233 / CIP 104796 / JCM 9543 / NBRC 105858 / Y-104)) Explore C8XA43 Go to UniProtKB: C8XA43 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | C8XA43 | ||||
Sequence AnnotationsExpand | |||||
| |||||
Small Molecules
| Ligands 3 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
| PGE Query on PGE | D [auth A] | TRIETHYLENE GLYCOL C6 H14 O4 ZIBGPFATKBEMQZ-UHFFFAOYSA-N |  | ||
| GOL Query on GOL | C [auth A], E [auth A] | GLYCEROL C3 H8 O3 PEDCQBHIVMGVHV-UHFFFAOYSA-N |  | ||
| ACY Query on ACY | B [auth A], F [auth A] | ACETIC ACID C2 H4 O2 QTBSBXVTEAMEQO-UHFFFAOYSA-N |  | ||
| Modified Residues 1 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Type | Formula | 2D Diagram | Parent |
| MSE Query on MSE | A | L-PEPTIDE LINKING | C5 H11 N O2 Se |  | MET |
Experimental Data & Validation
Experimental Data
- Method: X-RAY DIFFRACTION
- Resolution: 1.55 Å
- R-Value Free: 0.161
- R-Value Work: 0.141
- R-Value Observed: 0.142
- Space Group: P 43 21 2
Unit Cell:
| Length ( Å ) | Angle ( ˚ ) |
|---|---|
| a = 76.257 | α = 90 |
| b = 76.257 | β = 90 |
| c = 50.93 | γ = 90 |
| Software Name | Purpose |
|---|---|
| DENZO | data reduction |
| SCALEPACK | data scaling |
| MLPHARE | phasing |
| DM | phasing |
| REFMAC | refinement |
| PDB_EXTRACT | data extraction |
| SBC-Collect | data collection |
| HKL-3000 | data reduction |
| HKL-3000 | data scaling |
| HKL-3000 | phasing |
| SHELXD | phasing |
| SHELXE | model building |
| SOLVE | phasing |
| RESOLVE | phasing |
| ARP/wARP | model building |
| CCP4 | phasing |
| O | model building |
| Coot | model building |
Entry History
Deposition Data
- Released Date: 2012-10-17 Deposition Author(s): Cuff, M.E., Holowicki, J., Endres, M., Joachimiak, A., Midwest Center for Structural Genomics (MCSG)
Revision History (Full details and data files)
- Version 1.0: 2012-10-17
Type: Initial release - Version 1.1: 2017-11-15
Changes: Refinement description
