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PDB: 6 results

1GZB
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BU of 1gzb by Molmil
PEROXIDASE
Descriptor: 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, CALCIUM ION, PEROXIDASE, ...
Authors:Fukuyama, K, Kunishima, N, Amada, F.
Deposit date:1996-11-13
Release date:1997-03-12
Last modified:2020-07-29
Method:X-RAY DIFFRACTION (1.8 Å)
Cite:Pentacoordination of the heme iron of Arthromyces ramosus peroxidase shown by a 1.8 A resolution crystallographic study at pH 4.5.
FEBS Lett., 378, 1996
1ARW
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BU of 1arw by Molmil
CRYSTAL STRUCTURES OF CYANIDE-AND TRIIODIDE-BOUND FORMS OF ARTHROMYCES RAMOSUS PEROXIDASE AT DIFFERENT PH VALUES. PERTURBATIONS OF ACTIVE SITE RESIDUES AND THEIR IMPLICATION IN ENZYME CATALYSIS
Descriptor: 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, CALCIUM ION, CYANIDE ION, ...
Authors:Fukuyama, K, Kunishima, N, Amada, F.
Deposit date:1995-04-25
Release date:1996-01-29
Last modified:2020-07-29
Method:X-RAY DIFFRACTION (1.6 Å)
Cite:Crystal structures of cyanide- and triiodide-bound forms of Arthromyces ramosus peroxidase at different pH values. Perturbations of active site residues and their implication in enzyme catalysis.
J.Biol.Chem., 270, 1995
1ARV
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BU of 1arv by Molmil
CRYSTAL STRUCTURES OF CYANIDE-AND TRIIODIDE-BOUND FORMS OF ARTHROMYCES RAMOSUS PEROXIDASE AT DIFFERENT PH VALUES. PERTURBATIONS OF ACTIVE SITE RESIDUES AND THEIR IMPLICATION IN ENZYME CATALYSIS
Descriptor: 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, CALCIUM ION, CYANIDE ION, ...
Authors:Fukuyama, K, Kunishima, N, Amada, F.
Deposit date:1995-04-25
Release date:1996-01-29
Last modified:2020-07-29
Method:X-RAY DIFFRACTION (1.6 Å)
Cite:Crystal structures of cyanide- and triiodide-bound forms of Arthromyces ramosus peroxidase at different pH values. Perturbations of active site residues and their implication in enzyme catalysis.
J.Biol.Chem., 270, 1995
1ARU
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BU of 1aru by Molmil
CRYSTAL STRUCTURES OF CYANIDE-AND TRIIODIDE-BOUND FORMS OF ARTHROMYCES RAMOSUS PEROXIDASE AT DIFFERENT PH VALUES. PERTURBATIONS OF ACTIVE SITE RESIDUES AND THEIR IMPLICATION IN ENZYME CATALYSIS
Descriptor: 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, CALCIUM ION, CYANIDE ION, ...
Authors:Fukuyama, K, Kunishima, N, Amada, F.
Deposit date:1995-04-25
Release date:1996-01-29
Last modified:2020-07-29
Method:X-RAY DIFFRACTION (1.6 Å)
Cite:Crystal structures of cyanide- and triiodide-bound forms of Arthromyces ramosus peroxidase at different pH values. Perturbations of active site residues and their implication in enzyme catalysis.
J.Biol.Chem., 270, 1995
1ARX
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BU of 1arx by Molmil
CRYSTAL STRUCTURES OF CYANIDE-AND TRIIODIDE-BOUND FORMS OF ARTHROMYCES RAMOSUS PEROXIDASE AT DIFFERENT PH VALUES. PERTURBATIONS OF ACTIVE SITE RESIDUES AND THEIR IMPLICATION IN ENZYME CATALYSIS
Descriptor: 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, CALCIUM ION, IODIDE ION, ...
Authors:Fukuyama, K, Kunishima, N, Amada, F.
Deposit date:1995-04-25
Release date:1996-01-29
Last modified:2020-07-29
Method:X-RAY DIFFRACTION (1.9 Å)
Cite:Crystal structures of cyanide- and triiodide-bound forms of Arthromyces ramosus peroxidase at different pH values. Perturbations of active site residues and their implication in enzyme catalysis.
J.Biol.Chem., 270, 1995
1ARY
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BU of 1ary by Molmil
CRYSTAL STRUCTURES OF CYANIDE-AND TRIIODIDE-BOUND FORMS OF ARTHROMYCES RAMOSUS PEROXIDASE AT DIFFERENT PH VALUES. PERTURBATIONS OF ACTIVE SITE RESIDUES AND THEIR IMPLICATION IN ENZYME CATALYSIS
Descriptor: 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, CALCIUM ION, IODIDE ION, ...
Authors:Fukuyama, K, Kunishima, N, Amada, F.
Deposit date:1995-04-25
Release date:1996-01-29
Last modified:2020-07-29
Method:X-RAY DIFFRACTION (1.9 Å)
Cite:Crystal structures of cyanide- and triiodide-bound forms of Arthromyces ramosus peroxidase at different pH values. Perturbations of active site residues and their implication in enzyme catalysis.
J.Biol.Chem., 270, 1995

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