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- PDB-1php: STRUCTURE OF THE ADP COMPLEX OF THE 3-PHOSPHOGLYCERATE KINASE FRO... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1php | ||||||
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Title | STRUCTURE OF THE ADP COMPLEX OF THE 3-PHOSPHOGLYCERATE KINASE FROM BACILLUS STEAROTHERMOPHILUS AT 1.65 ANGSTROMS | ||||||
![]() | 3-PHOSPHOGLYCERATE KINASE | ||||||
![]() | KINASE | ||||||
Function / homology | ![]() phosphoglycerate kinase / phosphoglycerate kinase activity / glycolytic process / ATP binding / cytoplasm Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() | ||||||
![]() | Davies, G.J. / Watson, H.C. | ||||||
![]() | ![]() Title: Structure of the ADP complex of the 3-phosphoglycerate kinase from Bacillus stearothermophilus at 1.65 A. Authors: Davies, G.J. / Gamblin, S.J. / Littlechild, J.A. / Dauter, Z. / Wilson, K.S. / Watson, H.C. #1: ![]() Title: The Structure of a Thermally Stable 3-Phosphoglycerate Kinase and a Comparison with its Mesophilic Equivalent Authors: Davies, G.J. / Gamblin, S.J. / Littlechild, J.A. / Watson, H.C. #2: ![]() Title: Purification, Crystallisation and Preliminary X-Ray Analysis of the 3-Phosphoglycerate Kinase from Bacillus Stearothermophilus Authors: Davies, G.J. / Gamblin, S.J. / Littlechild, J.A. / Watson, H.C. #3: ![]() Title: Sequence and Expression of the Gene Encoding 3-Phosphoglycerate Kinase from Bacillus Stearothermophilus Authors: Davies, G.J. / Littlechild, J.A. / Watson, H.C. / Hall, L. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 106.9 KB | Display | ![]() |
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PDB format | ![]() | 78.7 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 719.4 KB | Display | ![]() |
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Full document | ![]() | 738.8 KB | Display | |
Data in XML | ![]() | 24.9 KB | Display | |
Data in CIF | ![]() | 38.9 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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Unit cell |
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Atom site foot note | 1: CIS PROLINE - PRO 188 |
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Components
#1: Protein | Mass: 42790.027 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() References: UniProt: P18912, phosphoglycerate kinase |
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#2: Chemical | ChemComp-MG / |
#3: Chemical | ChemComp-ADP / |
#4: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.36 Å3/Da / Density % sol: 47.84 % | ||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | *PLUS Temperature: 18 ℃ / pH: 7 / Method: vapor diffusion, hanging drop | ||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Radiation | Scattering type: x-ray |
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Radiation wavelength | Relative weight: 1 |
Reflection | *PLUS Highest resolution: 1.65 Å / Lowest resolution: 10 Å / Num. obs: 44754 / % possible obs: 94 % / Num. measured all: 119169 / Rmerge(I) obs: 0.056 / Biso Wilson estimate: 19 Å2 |
Reflection shell | *PLUS Highest resolution: 1.65 Å / Lowest resolution: 1.7 Å / Rmerge(I) obs: 0.156 |
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Processing
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Refinement | Resolution: 1.65→10 Å / σ(F): 0 /
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Refinement step | Cycle: LAST / Resolution: 1.65→10 Å
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Refine LS restraints |
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Refinement | *PLUS Num. reflection all: 44754 / Rfactor all: 0.156 / Rfactor Rwork: 0.156 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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