GlycoNAVI-Proteins is dataset of glycan and protein information. This is the content of GlycoNAVI.
Source | Last Updated |
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GlycoNAVI Proteins | December 11, 2024 |
PDB ID | UniProt ID | Title ▲ | Descriptor |
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7M72 | P11609 | MHC-like protein complex structure | |
7M72 | P01887 | MHC-like protein complex structure | |
7M72 | K7N5N2 | MHC-like protein complex structure | |
7M72 | 7M72 | MHC-like protein complex structure | |
7M72 | K7N5N2 | MHC-like protein complex structure | |
7M72 | 7M72 | MHC-like protein complex structure | |
7M72 | K7N5M4 | MHC-like protein complex structure | |
7M72 | K7N5M4 | MHC-like protein complex structure | |
1D3C | P43379 | MICHAELIS COMPLEX OF BACILLUS CIRCULANS STRAIN 251 CYCLODEXTRIN GLYCOSYLTRANSFERASE WITH GAMMA-CYCLODEXTRIN | |
1C81 | P07953 | MICHAELIS COMPLEX OF FRUCTOSE-2,6-BISPHOSPHATASE | |
1CE7 | 1CE7 | MISTLETOE LECTIN I FROM VISCUM ALBUM | |
1CE7 | P81830 | MISTLETOE LECTIN I FROM VISCUM ALBUM | |
2MLL | 2MLL | MISTLETOE LECTIN I FROM VISCUM ALBUM | |
2MLL | P81830 | MISTLETOE LECTIN I FROM VISCUM ALBUM | |
1SZ6 | P81446 | MISTLETOE LECTIN I FROM VISCUM ALBUM. CRYSTAL STRUCTURE AT 2.05 A RESOLUTION | |
2XZ5 | Q8WSF8 | MMTS-modified Y53C mutant of Aplysia AChBP in complex with acetylcholine | |
5MU9 | Q8X123 | MOA-E-64 complex | |
5D61 | Q8X123 | MOA-Z-VAD-fmk complex, direct orientation | |
5D61 | 5D61 | MOA-Z-VAD-fmk complex, direct orientation | |
5D62 | Q8X123 | MOA-Z-VAD-fmk complex, inverted orientation | |
5D62 | 5D62 | MOA-Z-VAD-fmk complex, inverted orientation | |
5D63 | Q8X123 | MOA-Z-VAD-fmk inhibitor complex, direct/inverted dual orientation | |
5D63 | 5D63 | MOA-Z-VAD-fmk inhibitor complex, direct/inverted dual orientation | |
1MHC | Q31093 | MODEL OF MHC CLASS I H2-M3 WITH NONAPEPTIDE FROM RAT ND1 REFINED AT 2.3 ANGSTROMS RESOLUTION | |
1MHC | P01887 | MODEL OF MHC CLASS I H2-M3 WITH NONAPEPTIDE FROM RAT ND1 REFINED AT 2.3 ANGSTROMS RESOLUTION | |
1MHC | P03889 | MODEL OF MHC CLASS I H2-M3 WITH NONAPEPTIDE FROM RAT ND1 REFINED AT 2.3 ANGSTROMS RESOLUTION | |
7LFI | Q31093 | MODEL OF MHC CLASS Ib H2-M3 WITH MOUSE ND1 N-TERMINAL HEPTAPEPTIDE REFINED AT 1.70 ANGSTROMS RESOLUTION | |
7LFI | P01887 | MODEL OF MHC CLASS Ib H2-M3 WITH MOUSE ND1 N-TERMINAL HEPTAPEPTIDE REFINED AT 1.70 ANGSTROMS RESOLUTION | |
7LFI | P03888 | MODEL OF MHC CLASS Ib H2-M3 WITH MOUSE ND1 N-TERMINAL HEPTAPEPTIDE REFINED AT 1.70 ANGSTROMS RESOLUTION | |
7LFJ | Q31093 | MODEL OF MHC CLASS Ib H2-M3 WITH MOUSE ND1 N-TERMINAL HEPTAPEPTIDE, ALA MUTANT, REFINED AT 1.70 ANGSTROMS RESOLUTION | |
7LFJ | P01887 | MODEL OF MHC CLASS Ib H2-M3 WITH MOUSE ND1 N-TERMINAL HEPTAPEPTIDE, ALA MUTANT, REFINED AT 1.70 ANGSTROMS RESOLUTION | |
7LFJ | P03888 | MODEL OF MHC CLASS Ib H2-M3 WITH MOUSE ND1 N-TERMINAL HEPTAPEPTIDE, ALA MUTANT, REFINED AT 1.70 ANGSTROMS RESOLUTION | |
7LFK | Q31093 | MODEL OF MHC CLASS Ib H2-M3 WITH MOUSE ND1 N-TERMINAL HEPTAPEPTIDE, THR MUTANT, REFINED AT 1.60 ANGSTROMS RESOLUTION | |
7LFK | P01887 | MODEL OF MHC CLASS Ib H2-M3 WITH MOUSE ND1 N-TERMINAL HEPTAPEPTIDE, THR MUTANT, REFINED AT 1.60 ANGSTROMS RESOLUTION | |
7LFK | P03888 | MODEL OF MHC CLASS Ib H2-M3 WITH MOUSE ND1 N-TERMINAL HEPTAPEPTIDE, THR MUTANT, REFINED AT 1.60 ANGSTROMS RESOLUTION | |
7LFL | Q31093 | MODEL OF MHC CLASS Ib H2-M3 WITH MOUSE ND1 N-TERMINAL HEPTAPEPTIDE, VAL MUTANT, MONOCLINIC CELL, REFINED AT 1.60 ANGSTROMS RESOLUTION | |
7LFL | P01887 | MODEL OF MHC CLASS Ib H2-M3 WITH MOUSE ND1 N-TERMINAL HEPTAPEPTIDE, VAL MUTANT, MONOCLINIC CELL, REFINED AT 1.60 ANGSTROMS RESOLUTION | |
7LFL | P03888 | MODEL OF MHC CLASS Ib H2-M3 WITH MOUSE ND1 N-TERMINAL HEPTAPEPTIDE, VAL MUTANT, MONOCLINIC CELL, REFINED AT 1.60 ANGSTROMS RESOLUTION | |
7LFM | Q31093 | MODEL OF MHC CLASS Ib H2-M3 WITH MOUSE ND1 N-TERMINAL HEPTAPEPTIDE, VAL MUTANT, TRICLINIC CELL, REFINED AT 1.60 ANGSTROMS RESOLUTION | |
7LFM | P01887 | MODEL OF MHC CLASS Ib H2-M3 WITH MOUSE ND1 N-TERMINAL HEPTAPEPTIDE, VAL MUTANT, TRICLINIC CELL, REFINED AT 1.60 ANGSTROMS RESOLUTION | |
7LFM | P03888 | MODEL OF MHC CLASS Ib H2-M3 WITH MOUSE ND1 N-TERMINAL HEPTAPEPTIDE, VAL MUTANT, TRICLINIC CELL, REFINED AT 1.60 ANGSTROMS RESOLUTION | |
1XIC | P24300 | MODES OF BINDING SUBSTRATES AND THEIR ANALOGUES TO THE ENZYME D-XYLOSE ISOMERASE | |
1XID | P24300 | MODES OF BINDING SUBSTRATES AND THEIR ANALOGUES TO THE ENZYME D-XYLOSE ISOMERASE | |
1XIE | P24300 | MODES OF BINDING SUBSTRATES AND THEIR ANALOGUES TO THE ENZYME D-XYLOSE ISOMERASE | |
1XIF | P24300 | MODES OF BINDING SUBSTRATES AND THEIR ANALOGUES TO THE ENZYME D-XYLOSE ISOMERASE | |
1XIG | P24300 | MODES OF BINDING SUBSTRATES AND THEIR ANALOGUES TO THE ENZYME D-XYLOSE ISOMERASE | |
1XIH | P24300 | MODES OF BINDING SUBSTRATES AND THEIR ANALOGUES TO THE ENZYME D-XYLOSE ISOMERASE | |
1XII | P24300 | MODES OF BINDING SUBSTRATES AND THEIR ANALOGUES TO THE ENZYME D-XYLOSE ISOMERASE | |
1BYH | Z25878 | MOLECULAR AND ACTIVE-SITE STRUCTURE OF A BACILLUS (1-3,1-4)-BETA-GLUCANASE | |
1MAA | P21836 | MOUSE ACETYLCHOLINESTERASE CATALYTIC DOMAIN, GLYCOSYLATED PROTEIN |
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Supported by JST NBDC Grant Number JPMJND2204
Partly supported by NIH Common Fund Grant #1U01GM125267-01
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Last updated: December 9, 2024