Structural Entry Filters:

Search Count: 12

Download
6WTN image
Human Jak2 Jh1 Domain In Complex With Ruxolitinib
Organism: Homo sapiens
Method: X-RAY DIFFRACTION
Resolution:1.83 Å Release Date: 2021-05-05
Classification: TRANSFERASE
Ligands: EDO, RXT

6WTO image
Human Jak2 Jh1 Domain In Complex With Baricitinib
Organism: Homo sapiens
Method: X-RAY DIFFRACTION
Resolution:1.74 Å Release Date: 2021-05-05
Classification: TRANSFERASE
Ligands: EDO, 3JW

6WTP image
Human Jak2 Jh1 Domain In Complex With Protac-Intermediate Linker Handle 3
Organism: Homo sapiens
Method: X-RAY DIFFRACTION
Resolution:2.50 Å Release Date: 2021-05-05
Classification: TRANSFERASE
Ligands: U8P, GOL

6WTQ image
Human Jak2 Jh1 Domain In Complex With Protac-Intermediate Linker Handle 4
Organism: Homo sapiens
Method: X-RAY DIFFRACTION
Resolution:1.80 Å Release Date: 2021-05-05
Classification: TRANSFERASE
Ligands: U8J, TRS, EDO

2NCA image
Structural Model For The N-Terminal Domain Of Human Cdc37

2XN0 image
Structure Of Alpha-Galactosidase From Lactobacillus Acidophilus Ncfm, Ptcl4 Derivative

2XN1 image
Structure Of Alpha-Galactosidase From Lactobacillus Acidophilus Ncfm With Tris

2XN2 image
Structure Of Alpha-Galactosidase From Lactobacillus Acidophilus Ncfm With Galactose

3GXK image
The Crystal Structure Of G-Type Lysozyme From Atlantic Cod (Gadus Morhua L.) In Complex With Nag Oligomers Sheds New Light On Substrate Binding And The Catalytic Mechanism. Native Structure To 1.9
Organism: Gadus morhua
Method: X-RAY DIFFRACTION
Resolution:1.90 Å Release Date: 2009-10-20
Classification: HYDROLASE
Ligands: CO

3GXR image
The Crystal Structure Of G-Type Lysozyme From Atlantic Cod (Gadus Morhua L.) In Complex With Nag Oligomers Sheds New Light On Substrate Binding And The Catalytic Mechanism. Structure With Nag To 1.7

3E2D image
The 1.4 A Crystal Structure Of The Large And Cold-Active Vibrio Sp. Alkaline Phosphatase

1LMN image
The Refined Crystal Structure Of Lysozyme From The Rainbow Trout (Oncorhynchus Mykiss)
Protein Functional Filters:
Feedback Form
Name
Email
Institute
Feedback