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- PDB-1scu: THE CRYSTAL STRUCTURE OF SUCCINYL-COA SYNTHETASE FROM ESCHERICHIA... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1scu | ||||||
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Title | THE CRYSTAL STRUCTURE OF SUCCINYL-COA SYNTHETASE FROM ESCHERICHIA COLI AT 2.5 ANGSTROMS RESOLUTION | ||||||
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![]() | LIGASE (ATP-BINDING) | ||||||
Function / homology | ![]() succinate-CoA ligase (GDP-forming) activity / succinate-CoA ligase complex (ADP-forming) / succinate-CoA ligase complex / succinate-CoA ligase (ADP-forming) / succinate-CoA ligase (ADP-forming) activity / succinyl-CoA metabolic process / tricarboxylic acid cycle / nucleotide binding / magnesium ion binding / ATP binding ...succinate-CoA ligase (GDP-forming) activity / succinate-CoA ligase complex (ADP-forming) / succinate-CoA ligase complex / succinate-CoA ligase (ADP-forming) / succinate-CoA ligase (ADP-forming) activity / succinyl-CoA metabolic process / tricarboxylic acid cycle / nucleotide binding / magnesium ion binding / ATP binding / cytoplasm / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() | ||||||
![]() | Wolodko, W.T. / Fraser, M.E. / James, M.N.G. / Bridger, W.A. | ||||||
![]() | ![]() Title: The crystal structure of succinyl-CoA synthetase from Escherichia coli at 2.5-A resolution. Authors: Wolodko, W.T. / Fraser, M.E. / James, M.N. / Bridger, W.A. #1: ![]() Title: Crystallization of Succinyl-Coa Synthetase from Escherichia Coli Authors: Wolodko, W.T. / James, M.N.G. / Bridger, W.A. | ||||||
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 257.2 KB | Display | ![]() |
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PDB format | ![]() | 213.8 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 537.9 KB | Display | ![]() |
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Full document | ![]() | 747.8 KB | Display | |
Data in XML | ![]() | 57.6 KB | Display | |
Data in CIF | ![]() | 81.3 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 A 121 / 2: CIS PROLINE - PRO B 42 / 3: CIS PROLINE - PRO B 200 / 4: CIS PROLINE - PRO D 121 / 5: CIS PROLINE - PRO E 42 / 6: CIS PROLINE - PRO E 200 7: RESIDUE 246 OF EACH ALPHA SUBUNIT IS A PHOSPHORYLATED HISTIDINE. |
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Components
#1: Protein | Mass: 29758.213 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() References: UniProt: P07459, UniProt: P0AGE9*PLUS, succinate-CoA ligase (ADP-forming) #2: Protein | Mass: 41438.496 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() References: UniProt: P0A836, succinate-CoA ligase (ADP-forming) #3: Chemical | #4: Water | ChemComp-HOH / | Sequence details | AMINO-TERMINAL ANALYSIS OF THE ALPHA SUBUNIT INDICATES THAT THE FIRST RESIDUE IS A SERINE (W. A. ...AMINO-TERMINAL ANALYSIS OF THE ALPHA SUBUNIT INDICATES THAT THE FIRST RESIDUE IS A SERINE (W. A. BRIDGE, ENZYMES, 3RD ED. 10, 581-606 (1974)). IN THE GENE SEQUENCING | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 3.41 Å3/Da / Density % sol: 63.93 % | |||||||||||||||||||||||||||||||||||
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Crystal grow | *PLUS Temperature: 21 ℃ / pH: 7.3 / Method: microdialysis / Details: Wolodko, W.T., (1984) J. Biol. Chem., 259, 5316. | |||||||||||||||||||||||||||||||||||
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 |
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Processing
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Refinement | Resolution: 2.5→100 Å / σ(F): 0 /
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Refinement step | Cycle: LAST / Resolution: 2.5→100 Å
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Refine LS restraints |
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