1N31

Structure of A Catalytically Inactive Mutant (K223A) of C-DES with a Substrate (Cystine) Linked to the Co-Factor

Summary for 1N31

Related1ELU 1ELQ 1N2T
DescriptorL-cysteine/cystine lyase C-DES, POTASSIUM ION, PYRIDOXAL-5'-PHOSPHATE, ... (5 entities in total)
Functional Keywordsinactive mutant, substrate complex, fe-s cluster synthesis, nifs-like, lyase
Biological sourceSynechocystis sp. PCC 6714
Total number of polymer chains2
Total molecular weight85824.86
Authors
Kaiser, J.T.,Bruno, S.,Clausen, T.,Huber, R.,Schiaretti, F.,Mozzarelli, A.,Kessler, D. (deposition date: 2002-10-25, release date: 2003-01-21, Last modification date: 2011-07-13)
Primary citation
Kaiser, J.T.,Bruno, S.,Clausen, T.,Huber, R.,Schiaretti, F.,Mozzarelli, A.,Kessler, D.
Snapshots of the Cystine Lyase "C-DES" during Catalysis: Studies in Solution and in the Crystalline State
J.Biol.Chem., 278:357-365, 2003
PubMed: 12386155 (PDB entries with the same primary citation)
DOI: 10.1074/jbc.M209862200
MImport into Mendeley
Experimental method
X-RAY DIFFRACTION (2.2 Å)
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Structure validation

ClashscoreRamachandran outliersSidechain outliers120 2.6%MetricValuePercentile RanksWorseBetterPercentile relative to all X-ray structuresPercentile relative to X-ray structures of similar resolution
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PDB entries from 2020-12-02