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Motion in Porphobilinogen Deaminase [pda]
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Classification Suspected Domain Motion, Hinge Mechanism [D-h-1]
Structures 1PDA Conformation 1 [ PartsList ]
Description Domains 1 and 2 similar to lactoferrin
Particular values describing motion Creation Date = 19970822 Modification Date = 19970822 Experimental Methods = x (Traditional x-ray)
References G V Louie, P D Brownlie, R Lambert, J B Cooper, T L Blundell, S P Wood, M J Warren, S C Woodcock and P M Jordan (1992). Structure of porphobilinogen deaminase reveals a flexible multidomain polymerase with a single catalytic site. Nature. 359: 33-39. [Medline info for 95094298]
GO terms associated with structures Molecular function hydroxymethylbilane synthase activity Biological process porphyrin biosynthesis
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Copyright 1995-2005 M. Gerstein, W. Krebs, S. Flores, N. Echols, and others
Email: Mark.Gerstein _at_ yale.edu