1DKU

CRYSTAL STRUCTURES OF BACILLUS SUBTILIS PHOSPHORIBOSYLPYROPHOSPHATE SYNTHETASE: MOLECULAR BASIS OF ALLOSTERIC INHIBITION AND ACTIVATION.

Summary for 1DKU

Related1DKR
DescriptorPROTEIN (PHOSPHORIBOSYL PYROPHOSPHATE SYNTHETASE), PHOSPHOMETHYLPHOSPHONIC ACID ADENOSYL ESTER, METHYL PHOSPHONIC ACID ADENOSINE ESTER, ... (4 entities in total)
Functional Keywordsopen alpha-beta structure, domain duplication, phosphoribosyltransferase type i fold, transferase
Biological sourceBacillus subtilis
Cellular locationCytoplasm  P14193
Total number of polymer chains2
Total molecular weight71361.4
Authors
Eriksen, T.A.,Kadziola, A.,Bentsen, A.-K.,Harlow, K.W.,Larsen, S. (deposition date: 1999-12-08, release date: 2000-04-05, Last modification date: 2017-10-04)
Primary citation
Eriksen, T.A.,Kadziola, A.,Bentsen, A.K.,Harlow, K.W.,Larsen, S.
Structural basis for the function of Bacillus subtilis phosphoribosyl-pyrophosphate synthetase.
Nat.Struct.Biol., 7:303-308, 2000
PubMed: 10742175 (PDB entries with the same primary citation)
DOI: 10.1038/74069
MImport into Mendeley
Experimental method
X-RAY DIFFRACTION (2.2 Å)
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Structure validation

ClashscoreRamachandran outliersSidechain outliersRSRZ outliers804.4%0.7%MetricValuePercentile RanksWorseBetterPercentile relative to all X-ray structuresPercentile relative to X-ray structures of similar resolution

More Asymmetric unit images

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