+Open data
-Basic information
Entry | Database: PDB / ID: 8it7 | ||||||
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Title | Phosphoglycerate mutase 1 complexed with a compound | ||||||
Components | Phosphoglycerate mutase 1 | ||||||
Keywords | ISOMERASE/INHIBITOR / ISOMERASE-INHIBITOR COMPLEX | ||||||
Function / homology | Function and homology information regulation of pentose-phosphate shunt / bisphosphoglycerate mutase / bisphosphoglycerate mutase activity / phosphoglycerate mutase activity / 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase activity / phosphoglycerate mutase (2,3-diphosphoglycerate-dependent) / respiratory burst / Gluconeogenesis / canonical glycolysis / Glycolysis ...regulation of pentose-phosphate shunt / bisphosphoglycerate mutase / bisphosphoglycerate mutase activity / phosphoglycerate mutase activity / 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase activity / phosphoglycerate mutase (2,3-diphosphoglycerate-dependent) / respiratory burst / Gluconeogenesis / canonical glycolysis / Glycolysis / regulation of glycolytic process / gluconeogenesis / glycolytic process / secretory granule lumen / ficolin-1-rich granule lumen / hydrolase activity / Neutrophil degranulation / protein kinase binding / extracellular exosome / extracellular region / membrane / cytosol / cytoplasm Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.8 Å | ||||||
Authors | Zhou, L. / Jiang, L.L. | ||||||
Funding support | China, 1items
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Citation | Journal: To Be Published Title: Phosphoglycerate mutase 1 complexed with a compound Authors: Zhou, L. / Jiang, L.L. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 8it7.cif.gz | 108.1 KB | Display | PDBx/mmCIF format |
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PDB format | pdb8it7.ent.gz | 81.9 KB | Display | PDB format |
PDBx/mmJSON format | 8it7.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/it/8it7 ftp://data.pdbj.org/pub/pdb/validation_reports/it/8it7 | HTTPS FTP |
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-Related structure data
Related structure data | 8it5C 8it6C 8it8C 8itbC 8itcC 8itdC C: citing same article (ref.) |
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Similar structure data | Similarity search - Function & homologyF&H Search |
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
#1: Protein | Mass: 29917.104 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: PGAM1, PGAMA, CDABP0006 / Production host: Escherichia coli (E. coli) References: UniProt: P18669, phosphoglycerate mutase (2,3-diphosphoglycerate-dependent), bisphosphoglycerate mutase #2: Chemical | ChemComp-CL / | #3: Chemical | ChemComp-MES / | #4: Chemical | ChemComp-Q9F / | Mass: 479.932 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C25H18ClNO5S / Feature type: SUBJECT OF INVESTIGATION Has ligand of interest | Y | |
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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: 2.98 Å3/Da / Density % sol: 58.69 % |
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Crystal grow | Temperature: 289 K / Method: vapor diffusion, hanging drop / Details: PEG3350, 100mM MES 6.0 |
-Data collection
Diffraction | Mean temperature: 100 K / Serial crystal experiment: N | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Diffraction source | Source: SYNCHROTRON / Site: SSRF / Beamline: BL18U1 / Wavelength: 0.97915 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Detector | Type: ADSC QUANTUM 315r / Detector: CCD / Date: Sep 21, 2021 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Radiation wavelength | Wavelength: 0.97915 Å / Relative weight: 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Reflection | Resolution: 2.8→50 Å / Num. obs: 17933 / % possible obs: 98.9 % / Redundancy: 12.9 % / CC1/2: 0.994 / CC star: 0.999 / Rmerge(I) obs: 0.239 / Rpim(I) all: 0.068 / Rrim(I) all: 0.249 / Χ2: 0.513 / Net I/σ(I): 2.6 / Num. measured all: 231246 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Reflection shell | Diffraction-ID: 1
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-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT / Resolution: 2.8→31.91 Å / SU ML: 0.29 / Cross valid method: THROUGHOUT / σ(F): 1.37 / Phase error: 24.33 / Stereochemistry target values: ML
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL | |||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.8→31.91 Å
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Refine LS restraints |
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LS refinement shell |
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