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The R15G mutant of human CX31.3/GJC3 connexin hemichannel

Analyse The R15G mutant of human CX31.3/GJC3 connexin hemichannel in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6L3V
Type: protein
Length: 1,206 residues
Chains: 6
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Gap junction gamma-3 protein
UniProt: Q8NFK1
Ligands: LMN
Pockets: 20 · best druggability 0.57

Structure

electron microscopy · 1 distinct chain · 70% helix, 6% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D, E, F	Gap junction gamma-3 protein	protein	201	70% helix, 6% strand	Q8NFK1

Ligands and binding sites

LMN · Lauryl Maltose Neopentyl Glycol · ligand · 6 copies · chains A, F, B, C, D, E

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

Pockets

20 pockets found on a 1 Å grid, 12 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	246	0.57	0.78	32	empty
2	243	0.56	0.78	24	empty
3	218	0.56	0.78	24	empty
4	232	0.55	0.77	30	empty
5	138	0.54	0.81	19	empty

Interfaces

6 interfaces between chains.

A–F · 1199 Å² buried · 5 hydrogen bonds · protein-protein
B–C · 1195 Å² buried · 5 hydrogen bonds · protein-protein
D–E · 1194 Å² buried · 5 hydrogen bonds · protein-protein
C–D · 1187 Å² buried · 5 hydrogen bonds · protein-protein
A–B · 1183 Å² buried · 5 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 18 disulfide (disulfide).

Compared structures

6L3V · The R15G mutant of human Cx31.3/GJC3 connexin hemichannel · the same entry in another collection · chain F against F, TM-score 1.00
Q8NFK1 · AlphaFold monomer V2.0 prediction for gap junction gamma-3 protein (Q8NFK1) · a predicted model of the same protein · chain E against A, TM-score 0.90

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 Q8NFK1
Elsewhere: RCSB PDB 6L3V · PDBe 6L3V · UniProt Q8NFK1

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