1M22

X-ray structure of native peptide amidase from Stenotrophomonas maltophilia at 1.4 A

Summary for 1M22

• Entry DOI: 10.2210/pdb1m22/pdb
• Related: 1M21
• Descriptor: peptide amidase, 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID (3 entities in total)
• Functional Keywords: eleven-stranded beta sheet, covered double layers of alpha helices on top and bottom, hydrolase
• Biological source: Stenotrophomonas maltophilia
• Total number of polymer chains: 2
• Total formula weight: 107567.21

Authors

Labahn, J.,Neumann, S.,Buldt, G.,Kula, M.-R.,Granzin, J. (deposition date: 2002-06-21, release date: 2002-10-16, Last modification date: 2024-03-13)

• Primary citation: Labahn, J.,Neumann, S.,Buldt, G.,Kula, M.-R.,Granzin, J.; An alternative mechanism for amidase signature enzymes; J.MOL.BIOL., 322:1053-1064, 2002; PubMed: 12367528; DOI: 10.1016/S0022-2836(02)00886-0

Experimental method

X-RAY DIFFRACTION (1.4 Å)