Crystal structure of C-phycocyanin of synechococcus vulcanus at 1.6 ångströms

Structure

x-ray diffraction · 2 distinct chains · 78% helix, 0% strand (DSSP).

Ligands and binding sites

• CYC · Phycocyanobilin · ligand · 2 copies · chains B, A
• BLA · Biliverdine IX alpha · ligand · chains A

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

Pockets

2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Interfaces

1 interface between chains.

• A–B · 1622 Ų buried · 14 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 3 cofactor, 1 modified (phycocyanobilin attachment, biliverdin attachment, nonstandard).

Compared structures

• 1KTP · Crystal structure of c-phycocyanin of synechococcus vulcanus at 1.6 angstroms · the same entry in another collection · chain A against A, TM-score 1.00
• P50032 · AlphaFold monomer V2.0 prediction for C-phycocyanin alpha subunit (P50032) · a predicted model of the same protein · chain A against A, TM-score 0.99
• P50033 · AlphaFold monomer V2.0 prediction for C-phycocyanin beta subunit (P50033) · a predicted model of the same protein · chain B against A, TM-score 0.99

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 P50032
• Every structure of UniProt P50033
• Elsewhere: RCSB PDB 1KTP · PDBe 1KTP · UniProt P50032 · UniProt P50033