Research workbench

Structure of full-length IP3R1 channel in the apo-state

Analyse Structure of full-length IP3R1 channel in the apo-state in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6MU2
Type: protein
Length: 8,680 residues
Chains: 4
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Inositol 1,4,5-trisphosphate receptor type 1
UniProt: P29994
Pockets: 20 · best druggability 0.82

Structure

electron microscopy · 1 distinct chain · 55% helix, 4% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
B, A, D, C	Inositol 1,4,5-trisphosphate receptor type 1	protein	2170	55% helix, 4% strand	P29994

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	775	0.82	0.84	63	empty
2	149	0.82	0.97	41	empty
3	1148	0.82	0.83	89	empty
4	143	0.81	0.97	39	empty
5	577	0.81	0.86	94	empty

Interfaces

6 interfaces between chains.

A–D · 3708 Å² buried · 23 hydrogen bonds · protein-protein
B–A · 3692 Å² buried · 28 hydrogen bonds · protein-protein
B–C · 3690 Å² buried · 24 hydrogen bonds · protein-protein
D–C · 3654 Å² buried · 26 hydrogen bonds · protein-protein
A–C · 172 Å² buried · 0 hydrogen bonds · protein-protein

Compared structures

6MU2 · Structure of full-length IP3R1 channel in the Apo-state · the same entry in another collection · chain B against B, 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 P29994
Elsewhere: RCSB PDB 6MU2 · PDBe 6MU2 · UniProt P29994

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.