Research workbench

Crystal structure of photoswitchable fluorescent protein PSMORANGE2

Analyse Crystal structure of photoswitchable fluorescent protein PSMORANGE2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4Q7U
Type: protein
Length: 217 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: PSMORANGE2
UniProt: D0VWW2
Ligands: OIM
Pockets: 2 · best druggability 0.83

Structure

x-ray diffraction · 1 distinct chain · 5% helix, 57% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	PSMORANGE2	protein	217	5% helix, 57% strand	D0VWW2

Ligands and binding sites

OIM · [(4Z)-2-{(2R,5R)-2-[(1S,2S)-1-amino-2-methylbutyl]-2-hydroxy-5-methyl-2,5-dihydro-1,3-oxazol-4-yl}-4-(4-hydroxybenzylidene)-5-oxo-4,5-dihydro-1H-imidazol-1-yl]acetic acid · ligand · chains A
GOL · Glycerol · additive · 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, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	190	0.83	0.97	39	OIM
2	58	0.35	0.78	21	empty

Modifications

Observed in the structure: 2 covalent (covalent ligand).

Compared structures

4Q7U · Crystal structure of photoswitchable fluorescent protein PSmOrange2 · 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 D0VWW2
Elsewhere: RCSB PDB 4Q7U · PDBe 4Q7U · UniProt D0VWW2

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.