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Thermostabilized phosphorylated chicken CFTR

Analyse Thermostabilized phosphorylated chicken CFTR in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6D3S
Type: protein
Length: 1,127 residues
Chains: 1
Method: electron microscopy
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 6.6
Source: Gallus gallus
Molecule: Cystic fibrosis transmembrane conductance regulator
EC: 3.6.3.49
UniProt: A0M8U4
Ligands: ATP
Pockets: 14 · best druggability 0.77

Structure

electron microscopy · resolution 6.6 · 1 distinct chain · 64% helix, 11% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Cystic fibrosis transmembrane conductance regulator (EC 3.6.3.49)	protein	1127	64% helix, 11% strand	A0M8U4

Ligands and binding sites

ATP · Adenosine-5'-triphosphate · ligand · 2 copies · chains A

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

Pockets

14 pockets found on a 1 Å grid, 9 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	702	0.77	0.83	89	empty
2	691	0.76	0.82	76	empty
3	783	0.75	0.80	115	empty
4	667	0.73	0.80	74	empty
5	615	0.70	0.79	83	empty

Compared structures

6D3S · Thermostabilized phosphorylated chicken cftr · 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 A0M8U4
Elsewhere: RCSB PDB 6D3S · PDBe 6D3S · UniProt A0M8U4

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