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1N31

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

Summary for 1N31
Entry DOI10.2210/pdb1n31/pdb
Related1ELQ 1ELU 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 formula 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: 2023-12-13)
Primary citationKaiser, 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
Cited by
PubMed: 12386155
DOI: 10.1074/jbc.M209862200
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.2 Å)
Structure validation

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