1ACM
ARGININE 54 IN THE ACTIVE SITE OF ESCHERICHIA COLI ASPARTATE TRANSCARBAMOYLASE IS CRITICAL FOR CATALYSIS: A SITE-SPECIFIC MUTAGENESIS, NMR AND X-RAY CRYSTALLOGRAPHY STUDY
1ACM の概要
エントリーDOI | 10.2210/pdb1acm/pdb |
分子名称 | ASPARTATE CARBAMOYLTRANSFERASE, CATALYTIC CHAIN, ASPARTATE CARBAMOYLTRANSFERASE REGULATORY CHAIN, N-(PHOSPHONACETYL)-L-ASPARTIC ACID, ... (5 entities in total) |
機能のキーワード | transferase (carbamoyl-p, aspartate) |
タンパク質・核酸の鎖数 | 4 |
化学式量合計 | 103288.14 |
構造登録者 | |
主引用文献 | Stebbins, J.W.,Robertson, D.E.,Roberts, M.F.,Stevens, R.C.,Lipscomb, W.N.,Kantrowitz, E.R. Arginine 54 in the active site of Escherichia coli aspartate transcarbamoylase is critical for catalysis: a site-specific mutagenesis, NMR, and X-ray crystallographic study. Protein Sci., 1:1435-1446, 1992 Cited by PubMed: 1303763主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (2.8 Å) |
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