Hcgc from methanococcus maripaludis cocrystallized with sah and pyridinol

Structure

x-ray diffraction · 4 distinct chains · 39% helix, 25% strand (DSSP).

Ligands and binding sites

• SAH · S-adenosyl-L-homocysteine · ligand · 4 copies · chains A, B, C, D
• 9KH · 6-carboxy methyl-4-hydroxy-2-pyridinol · ligand · 2 copies · chains A, B, C, D
• PJL · (3~{E})-3-[(~{E})-3-oxidanylprop-2-enoyl]iminopropanoic acid · ligand · chains A, B
• LI · Lithium ion · metal · 2 copies · chains A, C, D
• SO4 · Sulfate ion · ion · 4 copies · chains A, C, B, D
• PE4 · 2-{2-[2-(2-{2-[2-(2-ethoxy-ethoxy)-ethoxy]-ethoxy}-ethoxy)-ethoxy]-ethoxy}-ethanol · additive · 3 copies · chains A, B, C

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

15 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.

Interfaces

6 interfaces between chains.

• C–D · 1956 Ų buried · 23 hydrogen bonds · protein-protein
• A–B · 1927 Ų buried · 24 hydrogen bonds · protein-protein
• A–C · 836 Ų buried · 6 hydrogen bonds · protein-protein
• B–D · 676 Ų buried · 7 hydrogen bonds · protein-protein
• B–C · 304 Ų buried · 8 hydrogen bonds · protein-protein

Compared structures

• 5O4J · HcgC from Methanococcus maripaludis cocrystallized with SAH and pyridinol · the same entry in another collection · chain A against A, TM-score 1.00

Analyse

• Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
• Every structure of UniProt Q6LX54
• Elsewhere: RCSB PDB 5O4J · PDBe 5O4J · UniProt Q6LX54