Download MendeleyCrystal structure of putative beta-lactamase (NP_815223.1) from Enterococcus faecalis V583 at 1.50 A resolution
Joint Center for Structural Genomics (JCSG)To be published.
3CJM
Crystal structure of putative beta-lactamase (NP_815223.1) from Enterococcus faecalis V583 at 1.50 A resolution
- PDB DOI: https://doi.org/10.2210/pdb3CJM/pdb
- Classification: HYDROLASE
- Organism(s): Enterococcus faecalis V583
- Expression System: Escherichia coli
- Mutation(s): No
- Deposited: 2008-03-13 Released: 2008-03-25
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 1.50 Å
- R-Value Free: 0.172
- R-Value Work: 0.147
- R-Value Observed: 0.149
wwPDB Validation 3D Report Full Report
This is version 1.4 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 beta-lactamase | 282 | Enterococcus faecalis V583 | Mutation(s): 0 Gene Names: NP_815223.1, EF_1502 |  | |
UniProt | |||||
Find proteins for Q834X5 (Enterococcus faecalis (strain ATCC 700802 / V583)) Explore Q834X5 Go to UniProtKB: Q834X5 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | Q834X5 | ||||
Sequence AnnotationsExpand | |||||
| |||||
Small Molecules
| Ligands 2 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
| EDO Query on EDO | D [auth A] E [auth A] F [auth A] G [auth A] H [auth A] | 1,2-ETHANEDIOL C2 H6 O2 LYCAIKOWRPUZTN-UHFFFAOYSA-N |  | ||
| NO3 Query on NO3 | B [auth A], C [auth A] | NITRATE ION N O3 NHNBFGGVMKEFGY-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: 1.50 Å
- R-Value Free: 0.172
- R-Value Work: 0.147
- R-Value Observed: 0.149
- Space Group: P 41 21 2
- Diffraction Data: https://doi.org/10.18430/M33CJM
Unit Cell:
| Length ( Å ) | Angle ( ˚ ) |
|---|---|
| a = 64.975 | α = 90 |
| b = 64.975 | β = 90 |
| c = 140.905 | γ = 90 |
| Software Name | Purpose |
|---|---|
| REFMAC | refinement |
| PHENIX | refinement |
| SHELX | phasing |
| MolProbity | model building |
| SCALA | data scaling |
| PDB_EXTRACT | data extraction |
| ADSC | data collection |
| MOSFLM | data reduction |
| SHELXD | phasing |
| autoSHARP | phasing |
Entry History
Deposition Data
- Released Date: 2008-03-25 Deposition Author(s): Joint Center for Structural Genomics (JCSG)
Revision History (Full details and data files)
- Version 1.0: 2008-03-25
Type: Initial release - Version 1.1: 2011-07-13
Changes: Advisory, Source and taxonomy, Version format compliance - Version 1.2: 2017-10-25
Changes: Refinement description - Version 1.3: 2019-07-24
Changes: Data collection, Derived calculations, Refinement description - Version 1.4: 2023-02-01
Changes: Database references, Derived calculations
