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The chemical control of protein folding: engineering a superfolder green fluorescent protein

Analyse The chemical control of protein folding: engineering a superfolder green… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2Q6P
Type: protein
Length: 223 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Green fluorescent protein mutant 3
UniProt: Q93125
Ligands: CRO
Pockets: 1 · best druggability 0.77

Structure

x-ray diffraction · 1 distinct chain · 12% helix, 52% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Green fluorescent protein mutant 3	protein	223	12% helix, 52% strand	Q93125

Ligands and binding sites

CRO · {2-[(1R,2R)-1-amino-2-hydroxypropyl]-4-(4-hydroxybenzylidene)-5-oxo-4,5-dihydro-1H-imidazol-1-yl}acetic acid · ligand · chains A

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

Pockets

1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	103	0.77	0.97	26	CRO

Modifications

Observed in the structure: 10 modified, 2 cofactor (nonstandard, chromophore).

Compared structures

2Q6P · The Chemical Control of Protein Folding: Engineering a Superfolder Green Fluorescent… · 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 Q93125
Elsewhere: RCSB PDB 2Q6P · PDBe 2Q6P · UniProt Q93125

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