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6UBZ
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BU of 6ubz by Molmil
Crystal structure of D678A GoxA bound to glycine at pH 5.5
Descriptor: GLYCINE, MAGNESIUM ION, Uncharacterized protein GoxA
Authors:Yukl, E.T.
Deposit date:2019-09-13
Release date:2019-10-23
Last modified:2023-10-11
Method:X-RAY DIFFRACTION (1.83 Å)
Cite:Kinetic and structural evidence that Asp-678 plays multiple roles in catalysis by the quinoprotein glycine oxidase.
J.Biol.Chem., 294, 2019
6UC1
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BU of 6uc1 by Molmil
Crystal structure of D678A GoxA soaked in glycine at pH 7.5
Descriptor: GLYCINE, MAGNESIUM ION, SULFATE ION, ...
Authors:Yukl, E.T.
Deposit date:2019-09-13
Release date:2019-10-23
Last modified:2023-10-11
Method:X-RAY DIFFRACTION (2.19 Å)
Cite:Kinetic and structural evidence that Asp-678 plays multiple roles in catalysis by the quinoprotein glycine oxidase.
J.Biol.Chem., 294, 2019
6VMF
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BU of 6vmf by Molmil
Crystal structure of the Y766F mutant of GoxA soaked with glycine
Descriptor: Glycine oxidase, MAGNESIUM ION, SULFATE ION
Authors:Yukl, E.T.
Deposit date:2020-01-27
Release date:2020-04-08
Last modified:2023-10-11
Method:X-RAY DIFFRACTION (2.24 Å)
Cite:Roles of active-site residues in catalysis, substrate binding, cooperativity, and the reaction mechanism of the quinoprotein glycine oxidase.
J.Biol.Chem., 295, 2020
6VMW
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BU of 6vmw by Molmil
Crystal structure of the F316A mutant of GoxA soaked with glycine
Descriptor: Glycine oxidase, MAGNESIUM ION, SODIUM ION
Authors:Yukl, E.T.
Deposit date:2020-01-28
Release date:2020-04-08
Last modified:2023-10-11
Method:X-RAY DIFFRACTION (1.99 Å)
Cite:Roles of active-site residues in catalysis, substrate binding, cooperativity, and the reaction mechanism of the quinoprotein glycine oxidase.
J.Biol.Chem., 295, 2020
6VMV
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BU of 6vmv by Molmil
Crystal structure of the H767A mutant of GoxA soaked with glycine
Descriptor: Glycine oxidase, MAGNESIUM ION, SULFATE ION
Authors:Yukl, E.T.
Deposit date:2020-01-28
Release date:2020-04-08
Last modified:2023-10-11
Method:X-RAY DIFFRACTION (2.2 Å)
Cite:Roles of active-site residues in catalysis, substrate binding, cooperativity, and the reaction mechanism of the quinoprotein glycine oxidase.
J.Biol.Chem., 295, 2020
6VL7
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BU of 6vl7 by Molmil
Crystal structure of the H583C mutant of GoxA soaked with glycine
Descriptor: DI(HYDROXYETHYL)ETHER, Glycine oxidase, MAGNESIUM ION, ...
Authors:Yukl, E.T.
Deposit date:2020-01-22
Release date:2020-04-08
Last modified:2023-10-11
Method:X-RAY DIFFRACTION (2.14 Å)
Cite:Roles of active-site residues in catalysis, substrate binding, cooperativity, and the reaction mechanism of the quinoprotein glycine oxidase.
J.Biol.Chem., 295, 2020
1AAC
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BU of 1aac by Molmil
AMICYANIN OXIDIZED, 1.31 ANGSTROMS
Descriptor: AMICYANIN, COPPER (II) ION
Authors:Cunane, L.M, Chen, Z.-W, Durley, R.C.E, Mathews, F.S.
Deposit date:1995-09-07
Release date:1996-03-08
Last modified:2024-02-07
Method:X-RAY DIFFRACTION (1.31 Å)
Cite:X-ray structure of the cupredoxin amicyanin, from Paracoccus denitrificans, refined at 1.31 A resolution.
Acta Crystallogr.,Sect.D, 52, 1996
2MAD
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BU of 2mad by Molmil
THE ACTIVE SITE STRUCTURE OF METHYLAMINE DEHYDROGENASE: HYDRAZINES IDENTIFY C6 AS THE REACTIVE SITE OF THE TRYPTOPHAN DERIVED QUINONE COFACTOR
Descriptor: METHYLAMINE DEHYDROGENASE (HEAVY SUBUNIT), METHYLAMINE DEHYDROGENASE (LIGHT SUBUNIT)
Authors:Huizinga, E.G, Vellieux, F.M.D, Hol, W.G.J.
Deposit date:1992-05-20
Release date:1994-01-31
Last modified:2024-06-05
Method:X-RAY DIFFRACTION (2.25 Å)
Cite:Active site structure of methylamine dehydrogenase: hydrazines identify C6 as the reactive site of the tryptophan-derived quinone cofactor.
Biochemistry, 31, 1992
1MAE
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BU of 1mae by Molmil
The Active Site Structure of Methylamine Dehydrogenase: Hydrazines Identify C6 as the Reactive Site of the Tryptophan Derived Quinone Cofactor
Descriptor: METHYLAMINE DEHYDROGENASE (HEAVY SUBUNIT), METHYLAMINE DEHYDROGENASE (LIGHT SUBUNIT), NITROGEN MOLECULE
Authors:Huizinga, E.G, Vellieux, F.M.D, Hol, W.G.J.
Deposit date:1992-05-20
Release date:1994-01-31
Last modified:2024-06-05
Method:X-RAY DIFFRACTION (2.8 Å)
Cite:Active site structure of methylamine dehydrogenase: hydrazines identify C6 as the reactive site of the tryptophan-derived quinone cofactor.
Biochemistry, 31, 1992
1MAF
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BU of 1maf by Molmil
The Active Site Structure of Methylamine Dehydrogenase: Hydrazines Identify C6 as the Reactive Site of the Tryptophan Derived Quinone Cofactor
Descriptor: METHYLAMINE DEHYDROGENASE (HEAVY SUBUNIT), METHYLAMINE DEHYDROGENASE (LIGHT SUBUNIT), NITROGEN MOLECULE
Authors:Huizinga, E.G, Vellieux, F.M.D, Hol, W.G.J.
Deposit date:1992-05-20
Release date:1994-01-31
Last modified:2024-06-05
Method:X-RAY DIFFRACTION (2.6 Å)
Cite:Active site structure of methylamine dehydrogenase: hydrazines identify C6 as the reactive site of the tryptophan-derived quinone cofactor.
Biochemistry, 31, 1992
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數據於2025-07-09公開中

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