3KZM

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
Authors
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
X-RAY DIFFRACTION (1.95 Å)
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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
Download full validation reportDownload