Motion in Enolase [enolase]

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Classification Known Fragment Motion, Hinge Mechanism [F-h-2]

Structures
3ENL Conformation 1 [ PartsList ]
7ENL Conformation 2 [ PartsList ]

Description
Loop movements of ~7 Angstrom.

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

References
L Lebioda and B Stec (1991). Biochemistry. 30: 2817. [Medline info for 92294166]

GO terms associated with structures
Molecular functionphosphopyruvate hydratase activity
Cellular componentphosphopyruvate hydratase complex
Biological processglycolysis

Morphs

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Best representative
Morph Morph name Structure #1 Structure #2 Residues
3enl [ ] 7enl [ ] 436

User-submitted morphs
Morph Morph name Structure #1 Structure #2 Residues
05181-30974 Enolase 3enl [ A ] 7enl [ A ] 436
59941-23709 Enolase 7enl [ A ] 3enl [ A ] 436
99185-2807 Enolase 7enl [ A ] 3enl [ A ] 436
601674-27263 Enolase 3enl [ A ] 7enl [ A ] 436
31675-3687 Phosphofructokinase 3enl [ A ] 7enl [ A ] 436
85444-21268 TEST1 3enl [ A ] 7enl [ A ] 436

Automatic morphs
Morph Morph name Structure #1 Structure #2 Residues
va1oneA-4enlA Enolase 1one [ A ] 4enl [ A ] 436
va1oneA-3enlA Enolase 1one [ A ] 3enl [ A ] 436
va1oneB-5enlA Enolase 1one [ B ] 5enl [ A ] 436
va4enlA-1oneB Enolase (E.C. 4.2.1.11) (2-Pho 4enl [ A ] 1one [ B ] 436
va3enlA-1oneB Enolase (E.C. 4.2.1.11) (2-Pho 3enl [ A ] 1one [ B ] 436
va5enlA-1oneA Enolase (E.C. 4.2.1.11) (2-Pho 5enl [ A ] 1one [ A ] 436
va6enlA-1oneA Enolase (E.C. 4.2.1.11) (2-Pho 6enl [ A ] 1one [ A ] 436
va6enlA-1oneB Enolase (E.C. 4.2.1.11) (2-Pho 6enl [ A ] 1one [ B ] 436

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