Structural Entry Filters:

Search Count: 22

Download
9E2G image
Cryo-Em Structure Of 48 Nm Repeat Of Microtubule Doublet From T. Brucei Flagellum

9E5C image
Cryo-Em Structure Of 96 Nm Repeat Of Microtubule Doublet From T. Brucei Flagellum

8ZLD image
Crystal Structure Of Pfho From Plasmodium Falciparum At 2.78 A

7TXE image
Plasmodium Falciparum Cyt C2 Dsd

7U2V image
Plasmodium Falciparum Cyt C2 Dsd

7T5P image
Cryo-Em Structure Of Human Simc1-Slf2 Complex

7L78 image
H235C Variant Of Yeast Ferrochelatase

6V6A image
Inhibitory Scaffolding Of The Ancient Mapk, Erk7

6OIS image
Cryoem Structure Of Arabidopsis Dr Complex (Dms3-Rdm1)

6OIT image
Cryoem Structure Of Arabidopsis Ddr' Complex (Drd1 Peptide-Dms3-Rdm1)

5U9M image
Copper-Zinc Superoxide Dismutase Is Activated Through A Sulfenic Acid Intermediate At A Copper-Ion Entry Site

4QEN image
Crystal Structure Of Kryptonite In Complex With Mchh Dna And Sah

4QEO image
Crystal Structure Of Kryptonite In Complex With Mchh Dna, H3(1-15) Peptide And Sah

4QEP image
Crystal Structure Of Kryptonite In Complex With Mchg Dna And Sah

4ONJ image
Crystal Structure Of The Catalytic Domain Of Ntdrm

4ONQ image
Crystal Structure Of Ntdrm E283S/R309S/F310S/Y590S/D591S Mutant

4FSX image
Crystal Structure Of Se-Substituted Zea Mays Zmet2 In Complex With Sah
Organism: Zea mays
Method: X-RAY DIFFRACTION
Resolution:3.20 Å Release Date: 2012-10-17
Classification: TRANSFERASE
Ligands: SAH

4FT2 image
Crystal Structure Of Zea Mays Zmet2 In Complex H3(1-15)K9Me2 Peptide And Sah
Organism: Zea mays
Method: X-RAY DIFFRACTION
Resolution:3.20 Å Release Date: 2012-10-17
Classification: TRANSFERASE
Ligands: SAH

4FT4 image
Crystal Structure Of Zea Mays Zmet2 In Complex H3(1-32)K9Me2 Peptide And Sah
Organism: Zea mays
Method: X-RAY DIFFRACTION
Resolution:2.70 Å Release Date: 2012-10-17
Classification: TRANSFERASE
Ligands: SAH

4E8U image
Crystal Structure Of Arabidopsis Idn2 Xs Domain Along With A Small Segment Of Adjacent Coiled-Coil Region
Protein Functional Filters:
Feedback Form
Name
Email
Institute
Feedback