3KZM
Crystal structure of N-acetyl-L-ornithine transcarbamylase complexed with carbamyl phosphate
Replaces: 1ZQ2Summary for 3KZM
Entry DOI | 10.2210/pdb3kzm/pdb |
Related | 2FG7 3KZC 3KZK 3KZN 3KZO 3L02 3L04 3L05 3L06 |
Descriptor | N-acetylornithine carbamoyltransferase, PHOSPHORIC ACID MONO(FORMAMIDE)ESTER, GLYCEROL, ... (5 entities in total) |
Functional Keywords | transcarbamylase, amino-acid biosynthesis, arginine biosynthesis, cytoplasm, transferase |
Biological source | Xanthomonas campestris pv. campestris |
Cellular location | Cytoplasm (Probable): Q8P8J2 |
Total number of polymer chains | 1 |
Total formula weight | 40462.75 |
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.,Yu, X.,Roth, L.,Morizono, H.,Tuchman, M.,Allewell, N.M. Structures of N-acetylornithine transcarbamoylase from Xanthomonas campestris complexed with substrates and substrate analogs imply mechanisms for substrate binding and catalysis. Proteins, 64:532-542, 2006 Cited by PubMed: 16741992DOI: 10.1002/prot.21013 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.95 Å) |
Structure validation
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