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Photosynthetic reaction center mutant with tyr M 76 replaced with phe

Analyse Photosynthetic reaction center mutant with tyr M 76 replaced with phe in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1JGY
Type: protein
Length: 823 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Photosynthetic reaction center L subunit; Photosynthetic reaction center M subunit…
UniProt: P02954, P02953, P11846
Ligands: BCL, BPH, U10, SPO, CDL, FE
Pockets: 12 · best druggability 0.82

Structure

x-ray diffraction · 3 distinct chains · 51% helix, 10% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
L	Photosynthetic reaction center L subunit	protein	281	64% helix, 3% strand	P02954
M	Photosynthetic reaction center M subunit	protein	302	62% helix, 3% strand	P02953
H	Photosynthetic reaction center H subunit	protein	240	23% helix, 26% strand	P11846

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
SPO · Spheroidene · ligand · chains M
CDL · Cardiolipin · ligand · chains L, M, H
FE · Fe (III) ion · metal · chains L, M

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

Pockets

12 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1107	0.82	0.82	89	BCL
2	280	0.76	0.88	46	U10
3	75	0.73	0.97	22	empty
4	116	0.62	0.86	29	empty
5	222	0.59	0.80	31	SPO

Interfaces

3 interfaces between chains.

L–M · 4586 Å² buried · 60 hydrogen bonds · protein-protein
M–H · 2863 Å² buried · 41 hydrogen bonds · protein-protein
L–H · 1582 Å² buried · 20 hydrogen bonds · protein-protein

Compared structures

1JGY · Photosynthetic Reaction Center Mutant With Tyr M 76 Replaced With Phe · 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 1JGY · PDBe 1JGY · UniProt P02954 · UniProt P02953 · UniProt P11846

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