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GlycoNAVI Proteins
GlycoNAVI-Proteins is dataset of glycan and protein information. This is the content of GlycoNAVI.
| Source | Last Updated |
|---|---|
| GlycoNAVI Proteins | September 04, 2024 |
| PDB ID | UniProt ID | Title ▲ | Descriptor |
|---|---|---|---|
| 7USL | A5JW88 | Integrin alphaM/beta2 ectodomain in complex with adenylate cyclase toxin RTX751 and M1F5 Fab | |
| 7USL | 7USL | Integrin alphaM/beta2 ectodomain in complex with adenylate cyclase toxin RTX751 and M1F5 Fab | |
| 6MSU | P06756 | Integrin alphaVBeta3 in complex with EETI-II 2.5F | |
| 6MSU | P05106 | Integrin alphaVBeta3 in complex with EETI-II 2.5F | |
| 6MSU | 6MSU | Integrin alphaVBeta3 in complex with EETI-II 2.5F | |
| 1IZ2 | P01009 | Interactions causing the kinetic trap in serpin protein folding | |
| 1UR8 | Q54276 | Interactions of a family 18 chitinase with the designed inhibitor HM508, and its degradation product, chitobiono-delta-lactone | |
| 1UR9 | Q54276 | Interactions of a family 18 chitinase with the designed inhibitor HM508, and its degradation product, chitobiono-delta-lactone | |
| 2DSV | Q6TMG6 | Interactions of protective signalling factor with chitin-like polysaccharide: Crystal structure of the complex between signalling protein from sheep (SPS-40) and a hexasaccharide at 2.5A resolution | |
| 3LX9 | P06280 | Interconversion of Human Lysosomal Enzyme Specificities | |
| 3LXA | P06280 | Interconversion of Human Lysosomal Enzyme Specificities | |
| 3LXB | P06280 | Interconversion of Human Lysosomal Enzyme Specificities | |
| 3LXC | P06280 | Interconversion of Human Lysosomal Enzyme Specificities | |
| 6E3K | P01579 | Interferon gamma signalling complex with IFNGR1 and IFNGR2 | |
| 6E3K | P15260 | Interferon gamma signalling complex with IFNGR1 and IFNGR2 | |
| 6E3K | P38484 | Interferon gamma signalling complex with IFNGR1 and IFNGR2 | |
| 6E3L | P01579 | Interferon gamma signalling complex with IFNGR1 and IFNGR2 | |
| 6E3L | P15260 | Interferon gamma signalling complex with IFNGR1 and IFNGR2 | |
| 6E3L | P38484 | Interferon gamma signalling complex with IFNGR1 and IFNGR2 | |
| 8C7M | P42701 | Interleukin 12 receptor subunit beta-1 Fn domains in complex with antagonistic FAb fragment. | |
| 8C7M | 8C7M | Interleukin 12 receptor subunit beta-1 Fn domains in complex with antagonistic FAb fragment. | |
| 4NZD | Q9HBE5 | Interleukin 21 receptor | Interleukin-21 receptor |
| 8ENT | Q9HBE4 | Interleukin-21 signaling complex with IL-21R and IL-2Rg | |
| 8ENT | Q9HBE5 | Interleukin-21 signaling complex with IL-21R and IL-2Rg | |
| 8ENT | P31785 | Interleukin-21 signaling complex with IL-21R and IL-2Rg | |
| 5UV8 | P26951 | Interleukin-3 Receptor Complex | |
| 5UV8 | P08700 | Interleukin-3 Receptor Complex | |
| 3QB7 | D4HNR6 | Interleukin-4 mutant RGA bound to cytokine receptor common gamma | |
| 3QB7 | P31785 | Interleukin-4 mutant RGA bound to cytokine receptor common gamma | |
| 3EVJ | P01008 | Intermediate structure of antithrombin bound to the natural pentasaccharide | |
| 5HBC | P24627 | Intermediate structure of iron-saturated C-lobe of bovine lactoferrin at 2.79 Angstrom resolution indicates the softening of iron coordination | |
| 7BJ4 | D8J9C2 | Inulosucrase from Halalkalicoccus jeotgali bound to kestose | |
| 7BJC | D8J9C2 | Inulosucrase from Halalkalicoccus jeotgali in complex with sucrose | |
| 5B57 | B4EKB4 | Inward-facing conformation of ABC heme importer BhuUV from Burkholderia cenocepacia | |
| 5B57 | B4EKB5 | Inward-facing conformation of ABC heme importer BhuUV from Burkholderia cenocepacia | |
| 5ZOV | A0A1D7R1K6 | Inward-facing conformation of L-ascorbate transporter UlaA | |
| 6I1Q | A0A024S820 | Iodide structure of Trichoderma reesei Carbohydrate-Active Enzymes Family AA12 | Soluble quino protein glucose dehydrogenase |
| 2BXY | Q9RX51 | Is radiation damage dependent on the dose-rate used during macromolecular crystallography data collection | MALTOOLIGOSYLTREHALOSE TREHALOHYDROLASE (E.C.3.2.1.1) |
| 2BXY | 2BXY | Is radiation damage dependent on the dose-rate used during macromolecular crystallography data collection | MALTOOLIGOSYLTREHALOSE TREHALOHYDROLASE (E.C.3.2.1.1) |
| 2BXY | Q9RX51 | Is radiation damage dependent on the dose-rate used during macromolecular crystallography data collection | MALTOOLIGOSYLTREHALOSE TREHALOHYDROLASE (E.C.3.2.1.1) |
| 2BXY | 2BXY | Is radiation damage dependent on the dose-rate used during macromolecular crystallography data collection | MALTOOLIGOSYLTREHALOSE TREHALOHYDROLASE (E.C.3.2.1.1) |
| 2BXZ | Q9RX51 | Is radiation damage dependent on the dose-rate used during macromolecular crystallography data collection | MALTOOLIGOSYLTREHALOSE TREHALOHYDROLASE (E.C.3.2.1.1) |
| 2BXZ | 2BXZ | Is radiation damage dependent on the dose-rate used during macromolecular crystallography data collection | MALTOOLIGOSYLTREHALOSE TREHALOHYDROLASE (E.C.3.2.1.1) |
| 2BXZ | Q9RX51 | Is radiation damage dependent on the dose-rate used during macromolecular crystallography data collection | MALTOOLIGOSYLTREHALOSE TREHALOHYDROLASE (E.C.3.2.1.1) |
| 2BXZ | 2BXZ | Is radiation damage dependent on the dose-rate used during macromolecular crystallography data collection | MALTOOLIGOSYLTREHALOSE TREHALOHYDROLASE (E.C.3.2.1.1) |
| 2BY0 | Q9RX51 | Is radiation damage dependent on the dose-rate used during macromolecular crystallography data collection | MALTOOLIGOSYLTREHALOSE TREHALOHYDROLASE (E.C.3.2.1.1) |
| 2BY0 | 2BY0 | Is radiation damage dependent on the dose-rate used during macromolecular crystallography data collection | MALTOOLIGOSYLTREHALOSE TREHALOHYDROLASE (E.C.3.2.1.1) |
| 2BY0 | Q9RX51 | Is radiation damage dependent on the dose-rate used during macromolecular crystallography data collection | MALTOOLIGOSYLTREHALOSE TREHALOHYDROLASE (E.C.3.2.1.1) |
| 2BY0 | 2BY0 | Is radiation damage dependent on the dose-rate used during macromolecular crystallography data collection | MALTOOLIGOSYLTREHALOSE TREHALOHYDROLASE (E.C.3.2.1.1) |
| 2BY1 | Q9RX51 | Is radiation damage dependent on the dose-rate used during macromolecular crystallography data collection | MALTOOLIGOSYLTREHALOSE TREHALOHYDROLASE (E.C.3.2.1.1) |
