Crystal structure of N-acetyl-L-ornithine transcarbamylase complexed with carbamyl phosphate

Replaces:  1ZQ2

Summary for 3KZM

Related2FG7 3KZC 3KZK 3KZN 3KZO 3L02 3L04 3L05 3L06
DescriptorN-acetylornithine carbamoyltransferase, PHOSPHORIC ACID MONO(FORMAMIDE)ESTER, GLYCEROL, ... (5 entities in total)
Functional Keywordstranscarbamylase, amino-acid biosynthesis, arginine biosynthesis, cytoplasm, transferase
Biological sourceXanthomonas campestris pv. campestris
Cellular locationCytoplasm (Probable) Q8P8J2
Total number of polymer chains1
Total molecular weight40462.75
Shi, D.,Yu, X.,Allewell, N.M.,Tuchman, M. (deposition date: 2009-12-08, release date: 2010-03-31, Last modification date: 2011-07-13)
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
PubMed: 16741992 (PDB entries with the same primary citation)
DOI: 10.1002/prot.21013
MImport into Mendeley
Experimental method

Structure validation

RfreeClashscoreRamachandran outliersSidechain outliersRSRZ outliers0.22880.3%3.2%7.6%MetricValuePercentile RanksWorseBetterPercentile relative to all X-ray structuresPercentile relative to X-ray structures of similar resolution
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