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Spectroscopic and Structural Study of the Heterotropic Linkage between Halide and Proton Ion Binding to Gfp Proteins: E2(GFP)-Cl Complex

Analyse Spectroscopic and Structural Study of the Heterotropic Linkage between Halide… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2O24
Type: protein
Length: 236 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 1.45
Source: Aequorea victoria
Molecule: Green fluorescent protein
UniProt: P42212
Ligands: CL
Pockets: 2 · best druggability 0.73

Structure

x-ray diffraction · resolution 1.45 · 1 distinct chain · 11% helix, 50% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Green fluorescent protein	protein	236	11% helix, 50% strand	P42212

Ligands and binding sites

CL · Chloride ion · ion · 3 copies · 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	62	0.73	0.98	21	CL
2	77	0.34	0.75	16	empty

Compared structures

2O24 · Spectroscopic and structural study of the heterotropic linkage between halide and proton… · the same entry in another collection · chain A against A, TM-score 1.00
P42212 · AlphaFold monomer V2.0 prediction for green fluorescent protein (P42212) · a predicted model of the same protein · chain A against A, TM-score 0.95

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 P42212
Elsewhere: RCSB PDB 2O24 · PDBe 2O24 · UniProt P42212

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