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 |
---|---|---|---|
5AVX | Q4H132 | Kinetics by X-ray crystallography: Tl+-substitution of bound K+ in the E2.MgF42-.2K+ crystal after 20 min | |
5AVX | C4IX13 | Kinetics by X-ray crystallography: Tl+-substitution of bound K+ in the E2.MgF42-.2K+ crystal after 20 min | |
5AVX | Q70Q12 | Kinetics by X-ray crystallography: Tl+-substitution of bound K+ in the E2.MgF42-.2K+ crystal after 20 min | |
5AVY | Q4H132 | Kinetics by X-ray crystallography: Tl+-substitution of bound K+ in the E2.MgF42-.2K+ crystal after 20 min | |
5AVY | C4IX13 | Kinetics by X-ray crystallography: Tl+-substitution of bound K+ in the E2.MgF42-.2K+ crystal after 20 min | |
5AVY | Q70Q12 | Kinetics by X-ray crystallography: Tl+-substitution of bound K+ in the E2.MgF42-.2K+ crystal after 20 min | |
5AVW | Q4H132 | Kinetics by X-ray crystallography: Tl+-substitution of bound K+ in the E2.MgF42-.2K+ crystal after 16.5 min | |
5AVW | C4IX13 | Kinetics by X-ray crystallography: Tl+-substitution of bound K+ in the E2.MgF42-.2K+ crystal after 16.5 min | |
5AVW | Q70Q12 | Kinetics by X-ray crystallography: Tl+-substitution of bound K+ in the E2.MgF42-.2K+ crystal after 16.5 min | |
5AW3 | Q4H132 | Kinetics by X-ray crystallography: Tl+-substitution of bound K+ in the E2.MgF42-.2K+ crystal after 100 min | |
5AW3 | C4IX13 | Kinetics by X-ray crystallography: Tl+-substitution of bound K+ in the E2.MgF42-.2K+ crystal after 100 min | |
5AW3 | Q70Q12 | Kinetics by X-ray crystallography: Tl+-substitution of bound K+ in the E2.MgF42-.2K+ crystal after 100 min | |
5AVR | Q4H132 | Kinetics by X-ray crystallography: Tl+-substitution of bound K+ in the E2.MgF42-.2K+ crystal after 1.5 min | |
5AVR | C4IX13 | Kinetics by X-ray crystallography: Tl+-substitution of bound K+ in the E2.MgF42-.2K+ crystal after 1.5 min | |
5AVR | Q70Q12 | Kinetics by X-ray crystallography: Tl+-substitution of bound K+ in the E2.MgF42-.2K+ crystal after 1.5 min | |
5AVQ | Q4H132 | Kinetics by X-ray crystallography: Tl+-substitution of bound K+ in the E2.MgF42-.2K+ crystal after 0.75 min. | |
5AVQ | C4IX13 | Kinetics by X-ray crystallography: Tl+-substitution of bound K+ in the E2.MgF42-.2K+ crystal after 0.75 min. | |
5AVQ | Q70Q12 | Kinetics by X-ray crystallography: Tl+-substitution of bound K+ in the E2.MgF42-.2K+ crystal after 0.75 min. | |
5AW6 | Q4H132 | Kinetics by X-ray crystallography: Rb+-substitution of bound K+ in the E2.MgF42-.2K+ crystal after 5.5 min | |
5AW6 | C4IX13 | Kinetics by X-ray crystallography: Rb+-substitution of bound K+ in the E2.MgF42-.2K+ crystal after 5.5 min | |
5AW6 | Q70Q12 | Kinetics by X-ray crystallography: Rb+-substitution of bound K+ in the E2.MgF42-.2K+ crystal after 5.5 min | |
5AW5 | Q4H132 | Kinetics by X-ray crystallography: Rb+-substitution of bound K+ in the E2.MgF42-.2K+ crystal after 2.2 min | |
5AW5 | C4IX13 | Kinetics by X-ray crystallography: Rb+-substitution of bound K+ in the E2.MgF42-.2K+ crystal after 2.2 min | |
5AW5 | Q70Q12 | Kinetics by X-ray crystallography: Rb+-substitution of bound K+ in the E2.MgF42-.2K+ crystal after 2.2 min | |
5AW7 | Q4H132 | Kinetics by X-ray crystallography: Rb+-substitution of bound K+ in the E2.MgF42-.2K+ crystal after 11.3 min | |
5AW7 | C4IX13 | Kinetics by X-ray crystallography: Rb+-substitution of bound K+ in the E2.MgF42-.2K+ crystal after 11.3 min | |
5AW7 | Q70Q12 | Kinetics by X-ray crystallography: Rb+-substitution of bound K+ in the E2.MgF42-.2K+ crystal after 11.3 min | |
5AW4 | Q4H132 | Kinetics by X-ray crystallography: Rb+-substitution of bound K+ in the E2.MgF42-.2K+ crystal after 1.5 min | |
5AW4 | C4IX13 | Kinetics by X-ray crystallography: Rb+-substitution of bound K+ in the E2.MgF42-.2K+ crystal after 1.5 min | |
5AW4 | Q70Q12 | Kinetics by X-ray crystallography: Rb+-substitution of bound K+ in the E2.MgF42-.2K+ crystal after 1.5 min | |
5AW8 | Q4H132 | Kinetics by X-ray crystallography: E2.MgF42-.2RB+ crystal | |
5AW8 | C4IX13 | Kinetics by X-ray crystallography: E2.MgF42-.2RB+ crystal | |
5AW8 | Q70Q12 | Kinetics by X-ray crystallography: E2.MgF42-.2RB+ crystal | |
1XL0 | P00489 | Kinetic and crystallographic studies on 2-(beta-D-glucopyranosyl)-5-methyl-1,3,4-oxadiazole,-benzothiazole, and-benzimidazole, inhibitors of muscle glycogen phosphorylase b. Evidence for a new binding site. | Glycogen phosphorylase, muscle form (E.C.2.4.1.1) |
1XL1 | P00489 | Kinetic and crystallographic studies on 2-(beta-D-glucopyranosyl)-5-methyl-1,3,4-oxadiazole,-benzothiazole, and-benzimidazole, inhibitors of muscle glycogen phosphorylase b. Evidence for a new binding site. | Glycogen phosphorylase, muscle form (E.C.2.4.1.1) |
8B70 | P96589 | KimA from B. subtilis with nucleotide second-messenger c-di-AMP bound | |
5X3K | D2PPM7 | Kfla1895 D451A mutant in complex with isomaltose | |
5X3J | D2PPM7 | Kfla1895 D451A mutant in complex with cyclobis-(1->6)-alpha-nigerosyl | |
6F8N | A8GFD6 | Key residues affecting transglycosylation activity in family 18 chitinases - Insights into donor and acceptor subsites | |
2G1N | P00797 | Ketopiperazine-based renin inhibitors: Optimization of the "C" ring | Renin (E.C.3.4.23.15) |
2G1R | P00797 | Ketopiperazine-Based Renin Inhibitors: Optimization of the C Ring | Renin (E.C.3.4.23.15) |
2G1S | P00797 | Ketopiperazine-Based Renin Inhibitors: Optimization of the C Ring | Renin (E.C.3.4.23.15) |
2G1O | P00797 | Ketopiperazine-Based Renin Inhibitors: Optimization of the "C" Ring | Renin (E.C.3.4.23.15) |
2G1Y | P00797 | Ketopiperazine-Based Renin Inhibitors: Optimization of the "C" Ring | Renin (E.C.3.4.23.15) |
2G22 | P00797 | Ketopiperazine-Based Renin Inhibitors: Optimization of the "C" Ring | Renin (E.C.3.4.23.15) |
4PR7 | Q934G3 | KdgM porin in complex with disordered oligogalacturonate | |
7F57 | P42260 | Kainate-bound GluK2-1xNeto2 complex, at the desensitized state | |
7F57 | C6K2K4 | Kainate-bound GluK2-1xNeto2 complex, at the desensitized state | |
9B38 | P42260 | Kainate receptor GluK2 in complex with agonist glutamate with pseudo 4-fold symmetrical ligand-binding domain layer | |
9B39 | P42260 | Kainate receptor GluK2 in complex with agonist glutamate with asymmetric ligand-binding domain layer |
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
GlyCosmos Portal v4.0.0
Last updated: August 19, 2024