PROTEINS INVOLVED IN GLYCOLYSIS AND GLUCONEOGENESIS
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Aldolase A (E.C.4.1.2.13)
(1ald.pdb)
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Source: human (Homo sapiens) skeletal muscle
Authors: S. J. Gamblin, G. J. Davies, J. M. Grimes, R. M. Jackson, J. A.
Littlechild, H. C. Watson
Reference: "Activity and specificity of human aldolases",
J. Mol. Biol., 1991, 219, 573.
Triose phosphate isomerase (TIM) complexed with 2-phosphoglycolic acid
(1btm.pdb)
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Source: Bacillus stearothermophilus; expression system: Escherichia coli
Authors: F. Rentier-Delrue, S. C. Mande, S. Moyens, P. Terpstra, V. Mainfroid, K.
Goraj, M. Lion, W. G. J. Hol, J. A. Martial
Reference: "Cloning and over expression of the triosephosphate isomerase genes from
psychrophilic and thermophilic bacteria. Structural comparison of the predicted protein
sequences", J. Mol. Biol., 1995, 229, 85.
D-glyceraldehyde-3-phosphate dehydrogenase (holo form) (E.C.1.2.1.12) complexed with NAD
(1gga.pdb)
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Source: Trypanosoma brucei brucei, glycosome
Authors: F. M. D. Vellieux, J. Hajdu, C. L. M. J. Verlinde, H. Groendijr, R. J.
Read, T. J. Greenhough, J. W. Campbell, K. H. Kalk, J. A. Littlechild, H. C. Watson, W. G. J. Hol
Reference: "Structure of glycosomal glyceraldehyde-3-phosphate dehydrogenase",
Proc. Nat. Acad. Sci. USA, 1193, 90, 2355.
Phosphoglycerate kinase (E.C.2.7.2.3)
(2pgk.pdb)
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Source: Horse (Equus caballus) muscle
Authors: D. W. Rice
Reference: "The use of phase combination in the refinement of phosphoglycerate",
Acta Crystallogr., Sect. A, 1981, 37, 491.
Phosphoglycerate mutase (E.C.2.7.5.3) de-phospho enzyme complexed
with 3-phosphoglycerate and two sulphate ions
(3pgm.pdb)
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Source: dried baker's yeast (Saccharomyces cerevisiae)
Authors: S. I. Winn, H. C. Watson, R. N. Harkins, L. A. Fothergill
Reference: "Structure and activity of phosphoglycerate mutase",
Philos. Trans. R. Soc. Lond. B Biol. Sci. 1981, 293, 121.
Enolase (E.C.4.2.1.11) (2-phospho-D-glycerate hydrolase) complexed
with Mg2+
(1ebh.pdb)
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Source: baker's yeast (Saccharomyces cerevisiae)
Authors: J. E. Wedekind, G. H. Reed, I. Rayment
Reference: "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,
phosphonoacetohydroxamate, at Å 2.1 resolution",
Biochemistry, 1994, 33, 9333.
Pyruvate kinase in the T-state
(1pky.pdb)
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Source: Escherichia coli
Authors: A. Mattevi, G. Valentini, M. Rizzi, M. L. Speranza, M. Bolognesi, A. Coda
Reference: "Crystal structure of Escherichia coli pyruvate kinase type-I: molecular
bases of the allosteric transition",
Structure, 1995, 3, 729.
Fructose-1,6-bisphosphatase (E. C. 3.1.3.11) complex with
2,5-anhydroglucitol-1,6-bisphosphate and Zn2+
(1fbe.pdb)
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Source: Porcine (Sus scrofa) kidney cortex
Authors: Y. Zhang, J.-Y. Liang, S. Huang, H. Ke, W. N. Lipscomb
Reference: "Crystallographic studies of the catalytic mechanism of the neutral form
of fructose-1,6-bisphosphatase",
Biochemistry , 1993, 32, 1844.
Citations for the Protein Data Bank
The PDB files on this page were obtained from the
Protein Data Bank, and were created by the
authors listed above.
The Protein Data Bank, from
Research Collaboratory for Structural Bioinformatics is an archival
database of the three-dimensional structures of biological macromolecules
such as proteins, nucleic acids and carbohydrates. The stuctures are derived
from experimental work such as X-ray diffraction studies and NMR investigations.
Citations for the Protein Data Bank
The PDB files on this page were obtained from the
Protein Data Bank, and were created by the
authors listed above.
The Protein Data Bank, maintained by the
Research Collaboratory for Structural Bioinformatics is an archival
database of the three-dimensional structures of biological macromolecules
such as proteins, nucleic acids and carbohydrates. The stuctures are derived
from experimental work such as X-ray diffraction studies and NMR investigations.
The contents of PDB are in the public domain, but it is expected that
the authors of an entry as well as the PDB be properly cited whenever
their work is referred.
The following is the current citation for the PDB:
H.M.Berman, J.Westbrook, Z.Feng, G.Gilliland, T.N.Bhat, H.Weissig, I.N.Shindyalov,
P.E.Bourne "The Protein Data Bank" Nucleic Acids Research 2000, 28, 235-242.
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