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Monomeric crystal structure of RPBPHP1 photosensory core domain from the bacterium rhodopseudomonas palustris

Analyse Monomeric crystal structure of RPBPHP1 photosensory core domain from the… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5OY5
Type: protein
Length: 491 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: BPHP1
UniProt: A0A161I5N6
Ligands: BLA
Pockets: 4 · best druggability 0.83

Structure

x-ray diffraction · 1 distinct chain · 36% helix, 22% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	BPHP1	protein	491	36% helix, 22% strand	A0A161I5N6

Ligands and binding sites

BLA · Biliverdine IX alpha · ligand · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	360	0.83	0.92	48	BLA
2	381	0.58	0.75	45	empty
3	170	0.47	0.76	26	empty
4	66	0.41	0.80	20	empty

Modifications

Observed in the structure: 1 cofactor (biliverdin attachment).

Compared structures

5OY5 · Monomeric crystal structure of RpBphP1 photosensory core domain from the bacterium… · 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 A0A161I5N6
Elsewhere: RCSB PDB 5OY5 · PDBe 5OY5 · UniProt A0A161I5N6

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