- PDB-5pzq: Human liver fructose-1,6-bisphosphatase 1 (fructose 1,6-bisphosph... -
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Basic information
Entry
Database: PDB / ID: 5pzq
Title
Human liver fructose-1,6-bisphosphatase 1 (fructose 1,6-bisphosphate 1-phosphatase, E.C.3.1.3.11) complexed with the allosteric inhibitor 2-(4-methoxyphenyl)furan-3,4-dicarboxylic acid
Fructose-1,6-bisphosphatase1 / Growth-inhibiting protein 17 / cDNA FLJ75786 / highly similar to Homo sapiens fructose-1 / 6- ...Growth-inhibiting protein 17 / cDNA FLJ75786 / highly similar to Homo sapiens fructose-1 / 6-bisphosphatase 1 (FBP1) / mRNA
Mass: 36859.418 Da / Num. of mol.: 4 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: FBP1, hCG_1640493 / Production host: Escherichia coli (E. coli) References: UniProt: Q2TU34, UniProt: P09467*PLUS, fructose-bisphosphatase
Type: MAR CCD 165 mm / Detector: CCD / Date: Jun 7, 2005
Radiation
Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelength
Wavelength: 0.987 Å / Relative weight: 1
Reflection
Resolution: 2.7→41.277 Å / Num. obs: 36412 / % possible obs: 99.69 %
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Phasing
Phasing
Method: molecular replacement
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Processing
Software
Name
Version
Classification
NB
PHENIX
1.11.1_2575
refinement
PDB_EXTRACT
3.23
dataextraction
Refinement
Method to determine structure: MOLECULAR REPLACEMENT / Resolution: 2.7→41.277 Å / SU ML: 0.37 / Cross valid method: THROUGHOUT / σ(F): 1.38 / Phase error: 25.57 / Stereochemistry target values: ML / Details: INHIBITOR IN SUBUNIT D ONLY WEAKLY BOUND
Rfactor
Num. reflection
% reflection
Rfree
0.2333
1820
5 %
Rwork
0.1624
34592
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obs
0.166
36412
99.69 %
Solvent computation
Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL