Motion in Biotin carboxylase [bcbase]

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Classification [D-h-2]

Structures
1BNC [ PartsList ]
1DV2

Description
Observed motion in the b domain occurs as a result of ATP binding.

References
J B Thoden, C Z Blanchard, H M Holden, G L Waldrop (2000). Movement of the biotin carboxylase B-domain as a result of ATP binding. J Biol Chem, 275:16183-90 [Medline info for 10821865]
G L Waldrop, I Rayment, H M Holden (1994). Three-dimensional structure of the biotin carboxylase subunit of acetyl-CoA carboxylase. Biochemistry, 33:10249-56 [Medline info for 7915138]

GO terms associated with structures
Molecular functionbiotin binding, ligase activity, catalytic activity, ATP binding
Biological processmetabolism

Morphs

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Best representative
Morph Morph name Structure #1 Structure #2 Residues
Biotin Carboxylase 1bnc [ A ] 1dv2 [ A ] 452

User-submitted morphs
Morph Morph name Structure #1 Structure #2 Residues
755687-16118 Biotin Carboxylase 1bnc [ A ] 1dv2 [ A ] 452
698919-6821 Biotin Carboxylase 1dv1 [ A ] 1dv2 [ A ] 452


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