+Open data
-Basic information
Entry | Database: PDB / ID: 1a49 | ||||||
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Title | BIS MG-ATP-K-OXALATE COMPLEX OF PYRUVATE KINASE | ||||||
Components | PYRUVATE KINASE | ||||||
Keywords | TRANSFERASE / PYRUVATE KINASE / RABBIT MUSCLE / DOMAIN MOVEMENT / POTASSIUM BINDING | ||||||
Function / homology | Function and homology information pyruvate kinase / pyruvate kinase activity / positive regulation of cytoplasmic translation / positive regulation of sprouting angiogenesis / potassium ion binding / rough endoplasmic reticulum / non-specific protein-tyrosine kinase / cellular response to insulin stimulus / protein tyrosine kinase activity / non-specific serine/threonine protein kinase ...pyruvate kinase / pyruvate kinase activity / positive regulation of cytoplasmic translation / positive regulation of sprouting angiogenesis / potassium ion binding / rough endoplasmic reticulum / non-specific protein-tyrosine kinase / cellular response to insulin stimulus / protein tyrosine kinase activity / non-specific serine/threonine protein kinase / mRNA binding / magnesium ion binding / ATP binding / nucleus Similarity search - Function | ||||||
Biological species | Oryctolagus cuniculus (rabbit) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.1 Å | ||||||
Authors | Larsen, T.M. / Benning, M.M. / Rayment, I. / Reed, G.H. | ||||||
Citation | Journal: Biochemistry / Year: 1998 Title: Structure of the bis(Mg2+)-ATP-oxalate complex of the rabbit muscle pyruvate kinase at 2.1 A resolution: ATP binding over a barrel. Authors: Larsen, T.M. / Benning, M.M. / Rayment, I. / Reed, G.H. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1a49.cif.gz | 852.6 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1a49.ent.gz | 684.9 KB | Display | PDB format |
PDBx/mmJSON format | 1a49.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1a49_validation.pdf.gz | 844.6 KB | Display | wwPDB validaton report |
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Full document | 1a49_full_validation.pdf.gz | 1.1 MB | Display | |
Data in XML | 1a49_validation.xml.gz | 114 KB | Display | |
Data in CIF | 1a49_validation.cif.gz | 174.9 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/a4/1a49 ftp://data.pdbj.org/pub/pdb/validation_reports/a4/1a49 | HTTPS FTP |
-Related structure data
Related structure data | 1a5uC 1aqfS S: Starting model for refinement C: citing same article (ref.) |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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2 |
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Unit cell |
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-Components
-Protein , 1 types, 8 molecules ABCDEFGH
#1: Protein | Mass: 57998.820 Da / Num. of mol.: 8 / Source method: isolated from a natural source / Source: (natural) Oryctolagus cuniculus (rabbit) / Tissue: MUSCLE / References: UniProt: P11974, pyruvate kinase |
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-Non-polymers , 5 types, 1957 molecules
#2: Chemical | ChemComp-K / #3: Chemical | ChemComp-OXL / #4: Chemical | ChemComp-MG / #5: Chemical | ChemComp-ATP / #6: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.74 Å3/Da / Density % sol: 57.2 % | ||||||||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | pH: 6 / Details: pH 6.0 | ||||||||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Method: batch method | ||||||||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 113 K |
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Diffraction source | Source: SYNCHROTRON / Site: SSRL / Beamline: BL7-1 |
Detector | Date: Aug 1, 1996 |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Relative weight: 1 |
Reflection | Resolution: 2.1→30 Å / Num. obs: 267793 / % possible obs: 89 % |
Reflection shell | Resolution: 2.1→2.18 Å / Rsym value: 0.198 / % possible all: 78 |
Reflection | *PLUS Num. all: 301829 / Num. measured all: 815369 / Rmerge(I) obs: 0.047 |
Reflection shell | *PLUS % possible obs: 78 % / Rmerge(I) obs: 0.212 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB ENTRY 1AQF Resolution: 2.1→30 Å /
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Refinement step | Cycle: LAST / Resolution: 2.1→30 Å
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Refine LS restraints |
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Software | *PLUS Name: TNT / Version: 5D / Classification: refinement | ||||||||||||||||||||||||||||||
Refinement | *PLUS Rfactor obs: 0.198 | ||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||
Displacement parameters | *PLUS |