Download MendeleyCrystal structure of putative antidote protein of plasmid maintenance system (ZP_00107635.1) from Nostoc punctiforme PCC 73102 at 1.60 A resolution
Joint Center for Structural Genomics (JCSG)To be published.
3CEC
Crystal structure of a putative antidote protein of plasmid maintenance system (npun_f2943) from nostoc punctiforme pcc 73102 at 1.60 A resolution
- PDB DOI: https://doi.org/10.2210/pdb3CEC/pdb
- Classification: TRANSCRIPTION
- Organism(s): Nostoc punctiforme PCC 73102
- Expression System: Escherichia coli
- Mutation(s): No
- Deposited: 2008-02-28 Released: 2008-03-11
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 1.60 Å
- R-Value Free: 0.202
- R-Value Work: 0.166
- R-Value Observed: 0.168
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 antidote protein of plasmid maintenance system | 104 | Nostoc punctiforme PCC 73102 | Mutation(s): 0 Gene Names: ZP_00107635.1 |  | |
UniProt | |||||
Find proteins for D0VWT6 (Nostoc punctiforme (strain ATCC 29133 / PCC 73102)) Explore D0VWT6 Go to UniProtKB: D0VWT6 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | D0VWT6 | ||||
Sequence AnnotationsExpand | |||||
| |||||
Small Molecules
| Ligands 2 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
| MRD Query on MRD | B [auth A] | (4R)-2-METHYLPENTANE-2,4-DIOL C6 H14 O2 SVTBMSDMJJWYQN-RXMQYKEDSA-N |  | ||
| PEG Query on PEG | C [auth A] | DI(HYDROXYETHYL)ETHER C4 H10 O3 MTHSVFCYNBDYFN-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: 1.60 Å
- R-Value Free: 0.202
- R-Value Work: 0.166
- R-Value Observed: 0.168
- Space Group: P 1 21 1
- Diffraction Data: https://doi.org/10.18430/M33CEC
Unit Cell:
| Length ( Å ) | Angle ( ˚ ) |
|---|---|
| a = 35.07 | α = 90 |
| b = 36.71 | β = 98.38 |
| c = 50.05 | γ = 90 |
| Software Name | Purpose |
|---|---|
| REFMAC | refinement |
| PHENIX | refinement |
| SHELX | phasing |
| MolProbity | model building |
| XSCALE | data scaling |
| PDB_EXTRACT | data extraction |
| MAR345 | data collection |
| XDS | data reduction |
| SHELXD | phasing |
| autoSHARP | phasing |
Entry History
Deposition Data
- Released Date: 2008-03-11 Deposition Author(s): Joint Center for Structural Genomics (JCSG)
Revision History (Full details and data files)
- Version 1.0: 2008-03-11
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
