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PDBe Entry: 1c21 
E. COLI METHIONINE AMINOPEPTIDASE: METHIONINE COMPLEX
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HYDROLASE
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|
X-RAY DIFFRACTION
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Resolution: 1.8 Å, R-factor: 16.3%, Spacegroup: P 1 21 1
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17/11/1999, deposition: 22/07/1999, last revision: 24/02/2009
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Lowther, W.T.; Zhang, Y.; Sampson, P.B.; Honek, J.F.; Matthews, B.W.
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Insights into the mechanism of Escherichia coli methionine aminopeptidase from the structural analysis of reaction products and phosphorus-based transition-state analogues.
BIOCHEMISTRY vol:38, pag:14810-14819 (1999) [PubMed ID 10555963 ]
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PRODUCT COMPLEX, HYDROLASE
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3.4.11.18 ExPASy BRENDA (A)
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Escherichia coli 562(A)
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Methionine aminopeptidase (EC 3.4.11.18) (MAP) (Peptidase M) P0AE18 (A)
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|
A
|
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1mat, 2mat, 3mat, 4mat, 1c22, 1c23, 1c24, 1c27
|
| A |
METHIONINE AMINOPEPTIDASE |
Protein |
P0AE18 (AMPM_ECOLI)
|
263 |
99% |
|
| A |
COBALT (II) ION |
CO
|
| A |
SODIUM ION |
NA
|
| A |
METHIONINE |
MET
|
|
|
