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Full-length human TRPC3 in gdn

Analyse Full-length human TRPC3 in gdn in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6DJR
Type: protein
Length: 1,960 residues
Chains: 4
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Transient receptor potential cation channel subfamily C member 3
Pockets: 20 · best druggability 0.71

Structure

electron microscopy · 1 distinct chain · 73% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D	Transient receptor potential cation channel subfamily C member 3	protein	490	73% helix, 0% strand	—

Pockets

20 pockets found on a 1 Å grid, 15 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1124	0.71	0.75	121	empty
2	799	0.71	0.77	96	empty
3	1080	0.71	0.75	115	empty
4	985	0.70	0.75	105	empty
5	964	0.70	0.75	102	empty

Interfaces

4 interfaces between chains.

A–D · 427 Å² buried · 2 hydrogen bonds · protein-protein
A–B · 424 Å² buried · 2 hydrogen bonds · protein-protein
C–D · 424 Å² buried · 2 hydrogen bonds · protein-protein
B–C · 422 Å² buried · 2 hydrogen bonds · protein-protein

Compared structures

6DJR · Full-length human TRPC3 in GDN · 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 6DJR · PDBe 6DJR

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