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Open data
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Basic information
Entry | Database: PDB / ID: 6pfk | |||||||||
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Title | PHOSPHOFRUCTOKINASE, INHIBITED T-STATE | |||||||||
![]() | PHOSPHOFRUCTOKINASE | |||||||||
![]() | TRANSFERASE / KINASE / GLYCOLYSIS | |||||||||
Function / homology | ![]() 6-phosphofructokinase complex / 6-phosphofructokinase / 6-phosphofructokinase activity / fructose-6-phosphate binding / fructose 6-phosphate metabolic process / canonical glycolysis / monosaccharide binding / fructose 1,6-bisphosphate metabolic process / AMP binding / ATP binding ...6-phosphofructokinase complex / 6-phosphofructokinase / 6-phosphofructokinase activity / fructose-6-phosphate binding / fructose 6-phosphate metabolic process / canonical glycolysis / monosaccharide binding / fructose 1,6-bisphosphate metabolic process / AMP binding / ATP binding / identical protein binding / membrane / metal ion binding Similarity search - Function | |||||||||
Biological species | ![]() ![]() | |||||||||
Method | ![]() | |||||||||
![]() | Evans, P.R. / Schirmer, T. / Auer, M. | |||||||||
![]() | ![]() Title: Structural basis of the allosteric behaviour of phosphofructokinase. Authors: Schirmer, T. / Evans, P.R. | |||||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 245.4 KB | Display | ![]() |
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PDB format | ![]() | 198.4 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 466.8 KB | Display | ![]() |
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Full document | ![]() | 505.1 KB | Display | |
Data in XML | ![]() | 50.4 KB | Display | |
Data in CIF | ![]() | 68.7 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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1 |
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Unit cell |
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Noncrystallographic symmetry (NCS) | NCS oper:
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Components
#1: Protein | Mass: 34167.852 Da / Num. of mol.: 4 Source method: isolated from a genetically manipulated source Details: INHIBITED T-STATE Source: (gene. exp.) ![]() ![]() Gene: PFK / Plasmid: DERIVATIVE OF PBR322 / Gene (production host): PFK / Production host: ![]() ![]() #2: Chemical | ChemComp-PGA / #3: Water | ChemComp-HOH / | Sequence details | NON-CRYSTALLOGRAPHIC SYMMETRY WAS RE-IMPOSED BY REPLICATING SUBUNIT D (THE BEST DEFINED), THEN ...NON-CRYSTALLOG | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.68 Å3/Da / Density % sol: 54.02 % | ||||||||||||||||||||||||||||||
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Crystal grow | pH: 7.8 Details: THE CRYSTALS WERE GROWN FROM 1.6 - 1.8M POTASSIUM TARTRATE, PH 7.8, WITH 10MM 2-PHOSPHOGLYCOLATE, 0.5MM EDTA, 0.5MM DTT. THE CRYSTALS WERE GROWN FROM 1.6 - 1.8M POTASSIUM TARTRATE, PH 7.8, ...Details: THE CRYSTALS WERE GROWN FROM 1.6 - 1.8M POTASSIUM TARTRATE, PH 7.8, WITH 10MM 2-PHOSPHOGLYCOLATE, 0.5MM EDTA, 0.5MM DTT. THE CRYSTALS WERE GROWN FROM 1.6 - 1.8M POTASSIUM TARTRATE, PH 7.8, WITH 10MM 2-PHOSPHOGLYCOLATE, 0.5MM EDTA, 0.5MM DTT. 2-PHOSPHOGLYCOLATE IS AN ANALOGUE OF THE NATURAL ALLOSTERIC INHIBITOR PHOSPHOENOLPYRUVATE, SO THIS STRUCTURE REPRESENTS THE ALLOSTERICALLY INHIBITED T-STATE. THE ASYMMETRIC UNIT OF THE CRYSTAL IS THE TETRAMER WHICH OCCURS IN SOLUTION - CHAINS A, B, C, D. | ||||||||||||||||||||||||||||||
Crystal grow | *PLUS Method: unknown | ||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction source | Wavelength: 1.5418 |
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Detector | Type: MARRESEARCH |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2.6→20 Å / Num. obs: 44349 / % possible obs: 97 % / Redundancy: 3.5 % / Rmerge(I) obs: 0.126 |
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Processing
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Refinement | Resolution: 2.6→15 Å Details: DERIVED FROM ENGH & HUBER PARAMETERS BY V. LAMZIN FINAL RMS COORD. SHIFT 0.0095 ANGSTROMS
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Displacement parameters | Biso mean: 33 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.6→15 Å
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Refine LS restraints |
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Software | *PLUS Name: REFMAC / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Rfactor obs: 0.188 / Rfactor Rfree: 0.255 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS |