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Human connexin-26 (low pH closed conformation)

Analyse Human connexin-26 (low pH closed conformation) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6UVT
Type: protein
Length: 2,112 residues
Chains: 12
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Gap junction beta-2 protein
UniProt: P29033
Pockets: 14 · best druggability 0.62

Structure

electron microscopy · 1 distinct chain · 56% helix, 6% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, K, L, B, H, C, I, D, J, E, F, G	Gap junction beta-2 protein	protein	176	56% helix, 6% strand	P29033

Pockets

14 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	628	0.62	0.74	112	empty
2	559	0.60	0.74	98	empty
3	485	0.58	0.74	91	empty
4	428	0.56	0.74	85	empty
5	315	0.51	0.74	72	empty

Interfaces

18 interfaces between chains.

K–F · 158 Å² buried · 0 hydrogen bonds · protein-protein
J–E · 154 Å² buried · 0 hydrogen bonds · protein-protein
H–D · 152 Å² buried · 0 hydrogen bonds · protein-protein
L–G · 148 Å² buried · 0 hydrogen bonds · protein-protein
B–C · 148 Å² buried · 0 hydrogen bonds · protein-protein

Compared structures

6UVT · Human Connexin-26 (Low pH closed conformation) · the same entry in another collection · chain G against G, 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 P29033
Elsewhere: RCSB PDB 6UVT · PDBe 6UVT · UniProt P29033

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