Crystal structure of a standalone versatile eal protein from vibrio cholerae O395 - C-di-gmp bound form

Structure

x-ray diffraction · 1 distinct chain · 36% helix, 21% strand (DSSP).

Ligands and binding sites

• C2E · 9,9'-[(2r,3r,3as,5s,7ar,9r,10r,10as,12s,14ar)-3,5,10, 12-tetrahydroxy-5,12-dioxidooctahydro-2H,7H-difuro[3, 2-D:3',2'-J][1,3,7,9,2, 8]tetraoxadiphosphacyclododecine-2,9-diyl]bis(2-amino-1,9-dihydro-6H-purin-6-one) · ligand · 4 copies · chains A, B, C, D
• CA · Calcium ion · metal · 8 copies · chains A, B, C, D

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

Pockets

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

Interfaces

5 interfaces between chains.

• A–C · 1093 Ų buried · 11 hydrogen bonds · protein-protein
• B–D · 1080 Ų buried · 15 hydrogen bonds · protein-protein
• A–B · 563 Ų buried · 4 hydrogen bonds · protein-protein
• B–C · 153 Ų buried · 3 hydrogen bonds · protein-protein
• A–D · 151 Ų buried · 3 hydrogen bonds · protein-protein

Compared structures

• 6IH1 · Crystal structure of a standalone versatile EAL protein from Vibrio cholerae O395… · 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 A0A0H3AJ04
• Elsewhere: RCSB PDB 6IH1 · PDBe 6IH1 · UniProt A0A0H3AJ04