Photosynthetic reaction center mutant with ala M260 replaced with TRP (chain M, A260W)

Structure

x-ray diffraction · 3 distinct chains · 53% helix, 9% 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 · chains L, M
• SPN · Speroidenone · ligand · chains M
• CDL · Cardiolipin · ligand · chains H, L, M
• FE2 · Fe (II) ion · metal · chains L, M
• CL · Chloride ion · ion · chains M

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

Pockets

14 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

Interfaces

3 interfaces between chains.

• L–M · 4576 Ų buried · 70 hydrogen bonds · protein-protein
• H–M · 2878 Ų buried · 44 hydrogen bonds · protein-protein
• H–L · 1596 Ų buried · 16 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 1 covalent (covalent ligand).

Compared structures

• 1QOV · Photosynthetic reaction center mutant with ala M260 replaced with TRP (chain M, A260W) · the same entry in another collection · chain H against H, 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 P11846
• Every structure of UniProt P02954
• Every structure of UniProt P02953
• Elsewhere: RCSB PDB 1QOV · PDBe 1QOV · UniProt P11846 · UniProt P02954 · UniProt P02953