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1L8P
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MG-PHOSPHONOACETOHYDROXAMATE COMPLEX OF S39A YEAST ENOLASE 1
Descriptor:enolase 1, MAGNESIUM ION, PHOSPHONOACETOHYDROXAMIC ACID
Authors:Poyner, R.R., Larsen, T.M., Wong, S.W., Reed, G.H.
Deposit date:2002-03-21
Release date:2002-04-03
Last modified:2011-07-13
Method:X-RAY DIFFRACTION (2.1 Å)
Cite:Functional and structural changes due to a serine to alanine mutation in the active-site flap of enolase.
Arch.Biochem.Biophys., 401, 2002
1P43
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REVERSE PROTONATION IS THE KEY TO GENERAL ACID-BASE CATALYSIS IN ENOLASE
Descriptor:Enolase 1, MAGNESIUM ION, 2-PHOSPHOGLYCERIC ACID
Authors:Sims, P.A., Larsen, T.M., Poyner, R.R., Cleland, W.W., Reed, G.H.
Deposit date:2003-04-21
Release date:2003-11-18
Last modified:2017-10-11
Method:X-RAY DIFFRACTION (1.8 Å)
Cite:Reverse protonation is the key to general acid-base catalysis in enolase
Biochemistry, 42, 2003
1P48
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REVERSE PROTONATION IS THE KEY TO GENERAL ACID-BASE CATALYSIS IN ENOLASE
Descriptor:Enolase 1, MAGNESIUM ION, PHOSPHOENOLPYRUVATE
Authors:Sims, P.A., Larsen, T.M., Poyner, R.R., Cleland, W.W., Reed, G.H.
Deposit date:2003-04-21
Release date:2003-11-18
Last modified:2017-10-11
Method:X-RAY DIFFRACTION (2 Å)
Cite:Reverse protonation is the key to general acid-base catalysis in enolase
Biochemistry, 42, 2003
1EBG
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CHELATION OF SER 39 TO MG2+ LATCHES A GATE AT THE ACTIVE SITE OF ENOLASE: STRUCTURE OF THE BIS(MG2+) COMPLEX OF YEAST ENOLASE AND THE INTERMEDIATE ANALOG PHOSPHONOACETOHYDROXAMATE AT 2.1 ANGSTROMS RESOLUTION
Descriptor:ENOLASE, MAGNESIUM ION, PHOSPHONOACETOHYDROXAMIC ACID
Authors:Wedekind, J.E., Reed, G.H., Rayment, I.
Deposit date:1994-04-27
Release date:1995-04-27
Last modified:2011-07-13
Method:X-RAY DIFFRACTION (2.1 Å)
Cite:Chelation of serine 39 to Mg2+ latches a gate at the active site of enolase: structure of the bis(Mg2+) complex of yeast enolase and the intermediate analog phosphonoacetohydroxamate at 2.1-A resolution.
Biochemistry, 33, 1994
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