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- PDB-1e4y: Mutant P9L of adenylate kinase from E. coli, modified in the Gly-loop -
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Open data
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Basic information
Entry | Database: PDB / ID: 1e4y | ||||||
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Title | Mutant P9L of adenylate kinase from E. coli, modified in the Gly-loop | ||||||
![]() | Adenylate kinase | ||||||
![]() | TRANSFERASE(PHOSPHOTRANSFERASE) | ||||||
Function / homology | ![]() purine ribonucleotide interconversion / ADP biosynthetic process / nucleoside monophosphate metabolic process / CDP biosynthetic process / nucleoside diphosphate metabolic process / (d)CMP kinase activity / UMP kinase activity / adenylate kinase / adenylate kinase activity / AMP salvage ...purine ribonucleotide interconversion / ADP biosynthetic process / nucleoside monophosphate metabolic process / CDP biosynthetic process / nucleoside diphosphate metabolic process / (d)CMP kinase activity / UMP kinase activity / adenylate kinase / adenylate kinase activity / AMP salvage / UDP biosynthetic process / nucleoside diphosphate kinase activity / AMP binding / phosphorylation / magnesium ion binding / ATP binding / cytoplasm / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Mueller, C.W. / Schulz, G.E. | ||||||
![]() | ![]() Title: Crystal structures of two mutants of adenylate kinase from Escherichia coli that modify the Gly-loop. Authors: Muller, C.W. / Schulz, G.E. #1: Journal: J.Mol.Biol. / Year: 1990 Title: Induced-Fit Movements in Adenylate Kinases Authors: Schulz, G.E. / Mueller, C.W. / Diederichs, K. #2: Journal: J.Mol.Biol. / Year: 1988 Title: Structure of the Complex of Adenylate Kinase from Escherichia Coli with the Inhibitor P1, P5-Bis (Adenosine-5'-) Pentaphosphate Authors: Mueller, C.W. / Schulz, G.E. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 94.4 KB | Display | ![]() |
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PDB format | ![]() | 73 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 885.3 KB | Display | ![]() |
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Full document | ![]() | 905.3 KB | Display | |
Data in XML | ![]() | 18.8 KB | Display | |
Data in CIF | ![]() | 24.7 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
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Links
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Assembly
Deposited unit | ![]()
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1 | ![]()
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2 | ![]()
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Unit cell |
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Noncrystallographic symmetry (NCS) | NCS oper: (Code: given Matrix: (-0.995341, 0.068333, 0.068023), Vector: |
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Components
#1: Protein | Mass: 23678.150 Da / Num. of mol.: 2 / Mutation: L9P Source method: isolated from a genetically manipulated source Details: AP5A / Source: (gene. exp.) ![]() ![]() ![]() ![]() #2: Chemical | Compound details | CHAIN A, B ENGINEERED | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.85 Å3/Da / Density % sol: 56.84 % | ||||||||||||||||||||||||||||||||||||||||
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Crystal grow | pH: 7.2 / Details: pH 7.20 | ||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 20 ℃ / pH: 6.7 / Method: vapor diffusion, hanging drop | ||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 279 K |
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Diffraction source | Source: ![]() |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 3.4→10 Å / Num. obs: 7261 / % possible obs: 90 % / Observed criterion σ(I): 0 / Redundancy: 2 % / Rmerge(I) obs: 0.1 / Rsym value: 0.1 |
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Processing
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Refinement | Method to determine structure: ![]()
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Refinement step | Cycle: LAST / Resolution: 1.85→10 Å
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Refine LS restraints |
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