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Acid-tolerant monomeric GFP, gamillus, fluorescence (on) state

Analyse Acid-tolerant monomeric GFP, gamillus, fluorescence (on) state in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5Y00
Type: protein
Length: 229 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Green fluorescent protein
Ligands: CRQ, PO4, CL
Pockets: 1 · best druggability 0.73

Structure

x-ray diffraction · 1 distinct chain · 10% helix, 53% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Green fluorescent protein	protein	229	10% helix, 53% strand	—

Ligands and binding sites

CRQ · [2-(3-carbamoyl-1-imino-propyl)-4-(4-hydroxy-benzylidene)-5-oxo-4,5-dihydro-imidazol-1-yl]-acetic acid · ligand · chains A
PO4 · Phosphate ion · ion · chains A
CL · Chloride ion · ion · chains A
GOL · Glycerol · additive · 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	68	0.73	0.98	21	CRQ

Modifications

Observed in the structure: 2 cofactor (chromophore).

Compared structures

5Y00 · Acid-tolerant monomeric GFP, Gamillus, fluorescence (ON) state · 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
Elsewhere: RCSB PDB 5Y00 · PDBe 5Y00

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