Research workbench

Sfgfp mutant - 133 P-cyano-L-phenylalanine

Analyse Sfgfp mutant - 133 P-cyano-L-phenylalanine in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5DPG
Type: protein
Length: 232 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Green fluorescent protein
UniProt: A0A059PIQ0
Ligands: CRO, NA
Pockets: 1 · best druggability 0.76

Structure

x-ray diffraction · 1 distinct chain · 12% helix, 50% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Green fluorescent protein	protein	232	12% helix, 50% strand	A0A059PIQ0

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
NA · Sodium ion · metal · 2 copies · chains A
EDO · 1,2-ethanediol · additive · 10 copies · 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	78	0.76	0.98	23	CRO

Modifications

Observed in the structure: 2 cofactor, 1 modified (chromophore, nonstandard).

Compared structures

5DPG · sfGFP mutant - 133 p-cyano-L-phenylalanine · 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 A0A059PIQ0
Elsewhere: RCSB PDB 5DPG · PDBe 5DPG · UniProt A0A059PIQ0

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