Download MendeleyCRYSTAL STRUCTURE OF PHOSPHOGLYCERATE KINASE FROM PLASMODIUM FALCIPARUM
Chattopadhyay, D., Pal, B., Smith, C.D.To be published.
1LTK
CRYSTAL STRUCTURE OF PHOSPHOGLYCERATE KINASE FROM PLASMODIUM FALCIPARUM, IN THE OPEN CONFORMATION
- PDB DOI: https://doi.org/10.2210/pdb1LTK/pdb
- Classification: TRANSFERASE
- Organism(s): Plasmodium falciparum
- Expression System: Escherichia coli
- Mutation(s): No
- Deposited: 2002-05-20 Released: 2003-07-29
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 3.00 Å
- R-Value Free: 0.258
- R-Value Work: 0.208
- R-Value Observed: 0.284
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 |
| PHOSPHOGLYCERATE KINASE | 425 | Plasmodium falciparum | Mutation(s): 0 Gene Names: PGK EC: 2.7.2.3 |  | |
UniProt | |||||
Find proteins for P27362 (Plasmodium falciparum (isolate 3D7)) Explore P27362 Go to UniProtKB: P27362 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | P27362 | ||||
Sequence AnnotationsExpand | |||||
| |||||
Small Molecules
| Ligands 3 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
| AMP Query on AMP | E [auth A], H [auth B], J [auth C] | ADENOSINE MONOPHOSPHATE C10 H14 N5 O7 P UDMBCSSLTHHNCD-KQYNXXCUSA-N |  | ||
| SO4 Query on SO4 | D [auth A], G [auth B], I [auth C] | SULFATE ION O4 S QAOWNCQODCNURD-UHFFFAOYSA-L |  | ||
| GOL Query on GOL | F [auth A] | GLYCEROL C3 H8 O3 PEDCQBHIVMGVHV-UHFFFAOYSA-N |  | ||
| Modified Residues 1 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Type | Formula | 2D Diagram | Parent |
| MSE Query on MSE | A, B, C | L-PEPTIDE LINKING | C5 H11 N O2 Se |  | MET |
Experimental Data & Validation
Experimental Data
- Method: X-RAY DIFFRACTION
- Resolution: 3.00 Å
- R-Value Free: 0.258
- R-Value Work: 0.208
- R-Value Observed: 0.284
- Space Group: I 2 2 2
Unit Cell:
| Length ( Å ) | Angle ( ˚ ) |
|---|---|
| a = 119.03 | α = 90 |
| b = 147.61 | β = 90 |
| c = 206.49 | γ = 90 |
| Software Name | Purpose |
|---|---|
| HKL-2000 | data collection |
| SCALEPACK | data scaling |
| SOLVE | phasing |
| CNS | refinement |
| HKL-2000 | data reduction |
Entry History
Deposition Data
- Released Date: 2003-07-29 Deposition Author(s): Chattopadhyay, D., Pal, B., Smith, C.D.
Revision History (Full details and data files)
- Version 1.0: 2003-07-29
Type: Initial release - Version 1.1: 2008-04-28
Changes: Version format compliance - Version 1.2: 2011-07-13
Changes: Non-polymer description, Version format compliance
