Motion in Glycerate Dehydrogenase (GDH) [gdh]

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Classification Known Domain Motion, Hinge Mechanism [D-h-2]

Structures
1GDH H. methylovorum [ PartsList ]
1PSD E. coli [ PartsList ]

Description
Similiar to Formate Dehydrogenase (FDH)

Particular values describing motion
Experimental Methods = x (Traditional x-ray)
Creation Date = 19970822
Modification Date = 19970822

References
J D Goldberg, T Yoshida and P Brick (1994). Crystal structure of a NAD-dependent D-glycerate dehydrogenase at 2.4 A resolution. J Mol Biol. 236: 1123-40. [Medline info for 94166078]
Schuller, D. J., Grant, G. A., Banaszak, L. J. (1995). The allosteric ligand site in the Vmax-type cooperative enzyme phosphoglycerate dehydrogenase. Nat Struct Biol 2:69-76 [Medline info for 7719856]

GO terms associated with structures
Molecular functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor, amino acid binding
Biological processL-serine biosynthesis, metabolism

Morphs

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Best representative
Morph Morph name Structure #1 Structure #2 Residues
GDH 1gdh [ A ] 1psd [ A ] 409



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Copyright 1995-2005 M. Gerstein, W. Krebs, S. Flores, N. Echols, and others
Email: Mark.Gerstein _at_ yale.edu