2PHA

Crystal structure of native, unliganded human arginase at 1.90 resolution

Summary for 2PHA

Entry DOI	10.2210/pdb2pha/pdb
Related	1WVA 2AEB 2PHO
Descriptor	Arginase-1, MANGANESE (II) ION (3 entities in total)
Functional Keywords	proton wire, hydrolase
Biological source	Homo sapiens (human)
Cellular location	Cytoplasm: P05089
Total number of polymer chains	2
Total formula weight	69779.51
Authors	Di Costanzo, L.,Pique, M.E.,Christianson, D.W. (deposition date: 2007-04-10, release date: 2007-05-08, Last modification date: 2023-08-30)
Primary citation	Di Costanzo, L.,Pique, M.E.,Christianson, D.W. Crystal structure of human arginase I complexed with thiosemicarbazide reveals an unusual thiocarbonyl mu-sulfide ligand in the binuclear manganese cluster. J.Am.Chem.Soc., 129:6388-6389, 2007 Cited by PubMed Abstract: The crystal structure of the human arginase I-thiosemicarbazide complex reveals an unusual thiocarbonyl μ-sulfide ligand in the binuclear manganese cluster. The C=S moiety of thiosemicarbazide bridges MnA and MnB with coordination distances of 2.6 Å and 2.4 Å, respectively. Otherwise, the binding of thiosemicarbazide to human arginase I does not cause any significant structural changes in the active site. The crystal structure of the unliganded enzyme reveals a hydrogen bonded water molecule that could support proton transfer between a μ-water molecule and H141 to regenerate the nucleophilic μ-hydroxide ion in the final step of catalysis. PubMed: 17469833 DOI: 10.1021/ja071567j PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (1.9 Å)

Structure validation