3KZK
Crystal structure of acetylornithine transcarbamylase complexed with acetylcitrulline
Replaces: 1YH1Summary for 3KZK
Entry DOI | 10.2210/pdb3kzk/pdb |
Related | 2FG7 3KZC 3KZM 3KZN 3KZO 3L02 3L04 3L05 3L06 |
Descriptor | N-acetylornithine carbamoyltransferase, (S)-2-ACETAMIDO-5-UREIDOPENTANOIC ACID, SULFATE ION, ... (4 entities in total) |
Functional Keywords | transcarbamylase, amino-acid biosynthesis, arginine biosynthesis, cytoplasm, transferase |
Biological source | Xanthomonas campestris pv. campestris |
Cellular location | Cytoplasm : Q8P8J2 |
Total number of polymer chains | 1 |
Total formula weight | 40542.92 |
Authors | Shi, D.,Yu, X.,Allewell, N.M.,Tuchman, M. (deposition date: 2009-12-08, release date: 2010-03-31, Last modification date: 2023-11-22) |
Primary citation | Shi, D.,Morizono, H.,Yu, X.,Roth, L.,Caldovic, L.,Allewell, N.M.,Malamy, M.H.,Tuchman, M. Crystal structure of N-acetylornithine transcarbamylase from Xanthomonas campestris: a novel enzyme in a new arginine biosynthetic pathway found in several eubacteria. J.Biol.Chem., 280:14366-14369, 2005 Cited by PubMed: 15731101DOI: 10.1074/jbc.C500005200 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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