MolNFT v1 · #182697 · protein

Structure of tax-4_R421W apo open state

7N17 · Cyclic nucleotide-gated cation channel: “Structure of tax-4_R421W apo open state”. Electron microscopy, 1 ligand (CPL), 20 pockets (best druggability 0.81). MolNFT v1 #182697 on GenesisL1: 3D structure, binding sites and pockets in…

PDB: 7N17
Type: protein
Length: 2,068 residues
Chains: 4
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cyclic nucleotide-gated cation channel
UniProt: Q03611
Ligands: CPL
Pockets: 20 · best druggability 0.81

Structure

electron microscopy · 1 distinct chain · 52% helix, 12% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D	Cyclic nucleotide-gated cation channel	protein	517	52% helix, 12% strand	Q03611

Ligands and binding sites

CPL · 1-palmitoyl-2-linoleoyl-sn-glycero-3-phosphocholine · ligand · 24 copies · chains A, D, B, C

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

Pockets

20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	877	0.81	0.84	53	empty
2	697	0.70	0.77	60	empty
3	580	0.69	0.78	54	empty
4	576	0.68	0.78	54	empty
5	566	0.68	0.78	51	empty

Interfaces

6 interfaces between chains.

C–D · 2754 Å² buried · 28 hydrogen bonds · protein-protein
B–C · 2754 Å² buried · 27 hydrogen bonds · protein-protein
A–B · 2745 Å² buried · 27 hydrogen bonds · protein-protein
A–D · 2731 Å² buried · 28 hydrogen bonds · protein-protein
A–C · 25 Å² buried · 0 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 4 disulfide (disulfide).

Compared structures

7N17 · Structure of TAX-4_R421W apo open state · the same entry in another collection · chain D against D, TM-score 1.00
Q03611 · AlphaFold monomer V2.0 prediction for cyclic nucleotide-gated cation channel (Q03611) · a predicted model of the same protein · chain D against A, TM-score 0.93

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 Q03611
Elsewhere: RCSB PDB 7N17 · PDBe 7N17 · UniProt Q03611

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