Download MendeleyAlpha/beta hydrolase fold protein from Nakamurella multipartita.
Cuff, M.E., OSIPIUK, J., Holowicki, J., Endres, M., Joachimiak, A.To be published.
4Y7D
Alpha/beta hydrolase fold protein from Nakamurella multipartita
- PDB DOI: https://doi.org/10.2210/pdb4Y7D/pdb
- Classification: HYDROLASE
- Organism(s): Nakamurella multipartita DSM 44233
- Expression System: Escherichia coli BL21(DE3)
- Mutation(s): No
- Deposited: 2015-02-14 Released: 2015-02-25
- Funding Organization(s): National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 1.68 Å
- R-Value Free: 0.187
- R-Value Work: 0.153
- R-Value Observed: 0.155
wwPDB Validation 3D Report Full Report
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 |
| Alpha/beta hydrolase fold protein | 302 | Nakamurella multipartita DSM 44233 | Mutation(s): 0 Gene Names: Namu_0557 |  | |
UniProt | |||||
Find proteins for C8X7A4 (Nakamurella multipartita (strain ATCC 700099 / DSM 44233 / CIP 104796 / JCM 9543 / NBRC 105858 / Y-104)) Explore C8X7A4 Go to UniProtKB: C8X7A4 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | C8X7A4 | ||||
Sequence AnnotationsExpand | |||||
| |||||
Small Molecules
| Ligands 2 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
| CL Query on CL | C [auth A], E [auth B] | CHLORIDE ION Cl VEXZGXHMUGYJMC-UHFFFAOYSA-M |  | ||
| NA Query on NA | D [auth A], F [auth B] | SODIUM ION Na FKNQFGJONOIPTF-UHFFFAOYSA-N |  | ||
| 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: 1.68 Å
- R-Value Free: 0.187
- R-Value Work: 0.153
- R-Value Observed: 0.155
- Space Group: P 21 21 21
- Diffraction Data: https://doi.org/10.18430/M34Y7D
Unit Cell:
| Length ( Å ) | Angle ( ˚ ) |
|---|---|
| a = 67.404 | α = 90 |
| b = 75.394 | β = 90 |
| c = 126.536 | γ = 90 |
| Software Name | Purpose |
|---|---|
| HKL-3000 | data scaling |
| REFMAC | refinement |
| PDB_EXTRACT | data extraction |
| HKL-3000 | data reduction |
| HKL-3000 | phasing |
Entry History & Funding Information
Deposition Data
- Released Date: 2015-02-25 Deposition Author(s): Cuff, M.E., OSIPIUK, J., Holowicki, J., Endres, M., Joachimiak, A., Midwest Center for Structural Genomics (MCSG)
| Funding Organization | Location | Grant Number |
|---|---|---|
| National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS) | United States | GM094585 |
Revision History (Full details and data files)
- Version 1.0: 2015-02-25
Type: Initial release - Version 1.1: 2017-09-27
Changes: Advisory, Author supporting evidence, Derived calculations, Source and taxonomy, Structure summary - Version 1.2: 2019-12-25
Changes: Author supporting evidence
