2MAT

E.COLI METHIONINE AMINOPEPTIDASE AT 1.9 ANGSTROM RESOLUTION

Summary for 2MAT

Entry DOI	10.2210/pdb2mat/pdb
Descriptor	PROTEIN (METHIONINE AMINOPEPTIDASE), COBALT (II) ION, SODIUM ION, ... (4 entities in total)
Functional Keywords	hydrolase(alpha-aminoacylpeptide), hydrolase
Biological source	Escherichia coli
Total number of polymer chains	1
Total formula weight	29541.56
Authors	Lowther, W.T.,Orville, A.M.,Madden, D.T.,Lim, S.,Rich, D.H.,Matthews, B.W. (deposition date: 1999-03-29, release date: 1999-06-18, Last modification date: 2023-08-30)
Primary citation	Lowther, W.T.,Orville, A.M.,Madden, D.T.,Lim, S.,Rich, D.H.,Matthews, B.W. Escherichia coli methionine aminopeptidase: implications of crystallographic analyses of the native, mutant, and inhibited enzymes for the mechanism of catalysis. Biochemistry, 38:7678-7688, 1999 Cited by PubMed: 10387007 DOI: 10.1021/bi990684r PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (1.9 Å)

Structure validation