GlycoNAVI-Proteins is dataset of glycan and protein information. This is the content of GlycoNAVI.
PDB ID ▼ | UniProt ID | Title | Descriptor |
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X-RAY STRUCTURES AND MECHANISTIC IMPLICATIONS OF THREE FUNCTIONAL DERIVATIVES OF ASCORBATE OXIDASE FROM ZUCCHINI: REDUCED-, PEROXIDE-, AND AZIDE-FORMS
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ASCORBATE OXIDASE (REDUCED FORM) (E.C.1.10.3.3)
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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
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PEROXIDASE, PROTOPORPHYRIN IX CONTAINING FE
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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
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PEROXIDASE, PROTOPORPHYRIN IX CONTAINING FE
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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
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PEROXIDASE, PROTOPORPHYRIN IX CONTAINING FE
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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
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PEROXIDASE, PROTOPORPHYRIN IX CONTAINING FE
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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
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PEROXIDASE, PROTOPORPHYRIN IX CONTAINING FE
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Crystal structure of the fungal peroxidase from Arthromyces ramosus at 1.9 angstroms resolution: structural comparisons with the lignin and cytochrome C peroxidases
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PEROXIDASE (E.C.1.11.1.7)
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CRYSTAL STRUCTURE OF BOVINE BILE-SALT ACTIVATED LIPASE COMPLEXED WITH TAUROCHOLATE
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BARLEY 1,3-1,4-BETA-GLUCANASE IN MONOCLINIC SPACE GROUP
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HUMAN ASPARTYLGLUCOSAMINIDASE COMPLEX WITH REACTION PRODUCT
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ASPARTYLGLUCOSAMINIDASE, ASPARTATE
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GlyCosmos is a member of the GlySpace Alliance together with GlyGen and Glycomics@ExPASy.
Supported by JST NBDC Grant Number JPMJND2204
Partly supported by NIH Common Fund Grant #1U01GM125267-01