Download MendeleyThe structure of Synechococcus elongatus enolase reveals key aspects of phosphoenolpyruvate binding
Gonzalez, J.M., Marti-Arbona, R., Chen, J.C.-H., Unkefer, C.J.(2022) Acta Crystallogr F Struct Biol Commun F78: 177-184
5J04
Crystal structure of Enolase from Synechococcus elongatus, complex with phosphoenolpyruvate
- PDB DOI: https://doi.org/10.2210/pdb5J04/pdb
- Classification: LYASE
- Organism(s): Synechococcus elongatus PCC 7942 = FACHB-805
- Expression System: Escherichia coli
- Mutation(s): No
- Deposited: 2016-03-26 Released: 2016-04-20
- Funding Organization(s): National Scientific and Technical Research Council (CONICET)
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 2.30 Å
- R-Value Free: 0.245
- R-Value Work: 0.213
- R-Value Observed: 0.214
This is version 2.2 of the entry. See complete history.
Literature
Macromolecules
Find similar proteins by:
(by identity cutoff) | 3D Structure
Entity ID: 1 | |||||
|---|---|---|---|---|---|
| Molecule | Chains | Sequence Length | Organism | Details | Image |
| Enolase | 424 | Synechococcus elongatus PCC 7942 = FACHB-805 | Mutation(s): 0 Gene Names: eno, Synpcc7942_0639 EC: 4.2.1.11 |  | |
UniProt | |||||
Find proteins for Q5N3P4 (Synechococcus sp. (strain ATCC 27144 / PCC 6301 / SAUG 1402/1)) Explore Q5N3P4 Go to UniProtKB: Q5N3P4 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | Q5N3P4 | ||||
Sequence AnnotationsExpand | |||||
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Small Molecules
| Ligands 3 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
| PEP (Subject of Investigation/LOI) Query on PEP | C [auth A], I [auth B] | PHOSPHOENOLPYRUVATE C3 H5 O6 P DTBNBXWJWCWCIK-UHFFFAOYSA-N |  | ||
| ACT Query on ACT | H [auth A], M [auth B] | ACETATE ION C2 H3 O2 QTBSBXVTEAMEQO-UHFFFAOYSA-M |  | ||
| CA (Subject of Investigation/LOI) Query on CA | D [auth A] E [auth A] F [auth A] G [auth A] J [auth B] | CALCIUM ION Ca BHPQYMZQTOCNFJ-UHFFFAOYSA-N |  | ||
Experimental Data & Validation
Experimental Data
- Method: X-RAY DIFFRACTION
- Resolution: 2.30 Å
- R-Value Free: 0.245
- R-Value Work: 0.213
- R-Value Observed: 0.214
- Space Group: P 4 21 2
Unit Cell:
| Length ( Å ) | Angle ( ˚ ) |
|---|---|
| a = 164.23 | α = 90 |
| b = 164.23 | β = 90 |
| c = 72.68 | γ = 90 |
| Software Name | Purpose |
|---|---|
| REFMAC | refinement |
| Aimless | data scaling |
| PDB_EXTRACT | data extraction |
| iMOSFLM | data reduction |
| PHASER | phasing |
Entry History & Funding Information
Deposition Data
- Released Date: 2016-04-20 Deposition Author(s): Gonzalez, J.M.
| Funding Organization | Location | Grant Number |
|---|---|---|
| National Scientific and Technical Research Council (CONICET) | Argentina | PIP0024 |
Revision History (Full details and data files)
- Version 1.0: 2016-04-20
Type: Initial release - Version 2.0: 2022-04-13
Type: Coordinate replacement
Reason: Ligand identity
Changes: Advisory, Atomic model, Author supporting evidence, Data collection, Database references, Derived calculations, Non-polymer description, Other, Polymer sequence, Refinement description, Source and taxonomy, Structure summary - Version 2.1: 2023-09-27
Changes: Data collection, Refinement description - Version 2.2: 2024-02-28
Changes: Database references, Source and taxonomy
