MolNFT v1 · #156498 · protein

The cryo-EM structure of human pannexin 1

6M66 · Pannexin-1: “The cryo-EM structure of human pannexin 1”. Electron microscopy, 20 pockets (best druggability 0.84). MolNFT v1 #156498 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 6M66
Type: protein
Length: 1,855 residues
Chains: 7
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Pannexin-1
UniProt: Q96RD7
Pockets: 20 · best druggability 0.84

Structure

electron microscopy · 1 distinct chain · 63% helix, 2% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D, E, F, G	Pannexin-1	protein	265	63% helix, 2% strand	Q96RD7

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	1020	0.84	0.84	135	empty
2	968	0.83	0.84	126	empty
3	605	0.78	0.83	75	empty
4	472	0.76	0.84	66	empty
5	339	0.75	0.86	44	empty

Interfaces

7 interfaces between chains.

B–C · 1748 Å² buried · 13 hydrogen bonds · protein-protein
D–E · 1747 Å² buried · 14 hydrogen bonds · protein-protein
F–G · 1743 Å² buried · 13 hydrogen bonds · protein-protein
A–G · 1743 Å² buried · 13 hydrogen bonds · protein-protein
A–B · 1741 Å² buried · 12 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 14 disulfide (disulfide).

Compared structures

6M66 · The Cryo-EM Structure of Human Pannexin 1 · the same entry in another collection · chain G against G, TM-score 1.00
Q96RD7 · AlphaFold monomer V2.0 prediction for pannexin-1 (Q96RD7) · a predicted model of the same protein · chain A against A, TM-score 0.89

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 Q96RD7
Elsewhere: RCSB PDB 6M66 · PDBe 6M66 · UniProt Q96RD7

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