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GHK tagged GFP variant

Analyse GHK tagged GFP variant in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6QUJ
Type: protein
Length: 456 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 1.68
Source: Aequorea victoria
Molecule: Green fluorescent protein
UniProt: P42212
Ligands: CU, SO4
Pockets: 6 · best druggability 0.74

Structure

x-ray diffraction · resolution 1.68 · 1 distinct chain · 13% helix, 51% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
B, E	Green fluorescent protein	protein	228	13% helix, 51% strand	P42212

Ligands and binding sites

CU · Copper (II) ion · metal · 2 copies · chains B, E
SO4 · Sulfate ion · ion · 3 copies · chains B, E
GOL · Glycerol · additive · 2 copies · chains E

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

Pockets

6 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	78	0.74	0.97	24	empty
2	70	0.73	0.97	21	empty
3	75	0.46	0.82	13	empty
4	124	0.46	0.78	21	empty
5	103	0.46	0.80	25	SO4

Interfaces

1 interface between chains.

B–E · 728 Å² buried · 10 hydrogen bonds · protein-protein

Compared structures

P42212 · AlphaFold monomer V2.0 prediction for green fluorescent protein (P42212) · a predicted model of the same protein · chain B against A, TM-score 0.99

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 6QUJ · PDBe 6QUJ · UniProt P42212

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