Photosynthetic reaction center mutant with phe M 197 replaced with arg and tyr M 177 replaced with phe (chain M, Y177F, F197R)

Structure

x-ray diffraction · 3 distinct chains · 53% helix, 10% strand (DSSP).

Ligands and binding sites

• BCL · Bacteriochlorophyll A · ligand · 4 copies · chains L, M
• BPH · Bacteriopheophytin A · ligand · 2 copies · chains L, M
• U10 · Ubiquinone-10 · ligand · 2 copies · chains L, M
• SPN · Speroidenone · ligand · chains M
• FE2 · Fe (II) ion · metal · chains L, M
• PO4 · Phosphate ion · ion · chains L, M
• LDA · Lauryl dimethylamine-N-oxide · additive · 3 copies · chains M, H, L

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

Pockets

15 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.

Interfaces

3 interfaces between chains.

• L–M · 4552 Ų buried · 63 hydrogen bonds · protein-protein
• M–H · 2824 Ų buried · 40 hydrogen bonds · protein-protein
• L–H · 1622 Ų buried · 13 hydrogen bonds · protein-protein

Compared structures

• 1MPS · Photosynthetic reaction center mutant with phe M 197 replaced with arg and tyr M 177… · the same entry in another collection · chain L against L, 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 P02954
• Every structure of UniProt P02953
• Every structure of UniProt P11846
• Elsewhere: RCSB PDB 1MPS · PDBe 1MPS · UniProt P02954 · UniProt P02953 · UniProt P11846