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1C22

E. COLI METHIONINE AMINOPEPTIDASE: TRIFLUOROMETHIONINE COMPLEX

Summary for 1C22
Entry DOI10.2210/pdb1c22/pdb
Related1C21 1C23 1C24 1C27 1MAT 2MAT 3MAT 4MAT
DescriptorMETHIONINE AMINOPEPTIDASE, COBALT (II) ION, SODIUM ION, ... (5 entities in total)
Functional Keywordsproduct complex, hydrolase
Biological sourceEscherichia coli
Total number of polymer chains1
Total formula weight29554.62
Authors
Lowther, W.T.,Zhang, Y.,Sampson, P.B.,Honek, J.F.,Matthews, B.W. (deposition date: 1999-07-22, release date: 1999-11-17, Last modification date: 2024-02-07)
Primary citationLowther, W.T.,Zhang, Y.,Sampson, P.B.,Honek, J.F.,Matthews, B.W.
Insights into the mechanism of Escherichia coli methionine aminopeptidase from the structural analysis of reaction products and phosphorus-based transition-state analogues.
Biochemistry, 38:14810-14819, 1999
Cited by
PubMed: 10555963
DOI: 10.1021/bi991711g
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.75 Å)
Structure validation

218853

数据于2024-04-24公开中

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