4FCK
Crystal Structure of the Co2+2-Human Arginase I-AGPA Complex
Summary for 4FCK
| Entry DOI | 10.2210/pdb4fck/pdb |
| Related | 2PHA 4FCI |
| Descriptor | Arginase-1, 2-AMINO-3-GUANIDINO-PROPIONIC ACID, COBALT (II) ION, ... (4 entities in total) |
| Functional Keywords | arginase fold, hydrolase, hydrolase-hydrolase inhibitor complex, hydrolase/hydrolase inhibitor |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 2 |
| Total formula weight | 70087.79 |
| Authors | D'Antonio, E.L.,Christianson, D.W. (deposition date: 2012-05-25, release date: 2012-06-20, Last modification date: 2023-09-13) |
| Primary citation | D'Antonio, E.L.,Christianson, D.W. Binding of the unreactive substrate analog L-2-amino-3-guanidinopropionic acid (dinor-L-arginine) to human arginase I. Acta Crystallogr.,Sect.F, 68:889-893, 2012 Cited by PubMed Abstract: Human arginase I (HAI) is a binuclear manganese metalloenzyme that catalyzes the hydrolysis of L-arginine to form L-ornithine and urea through a metal-activated hydroxide mechanism. Since HAI regulates L-Arg bioavailability for NO biosynthesis, it is a potential drug target for the treatment of cardiovascular diseases such as atherosclerosis. X-ray crystal structures are now reported of the complexes of Mn(2)(2+)-HAI and Co(2)(2+)-HAI with L-2-amino-3-guanidinopropionic acid (AGPA; also known as dinor-L-arginine), an amino acid bearing a guanidinium side chain two methylene groups shorter than that of L-arginine. Hydrogen bonds to the α-carboxylate and α-amino groups of AGPA dominate enzyme-inhibitor recognition; the guanidinium group does not interact directly with the metal ions. PubMed: 22869115DOI: 10.1107/S1744309112027820 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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