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Structure of calcium-bound MTMEM16A(AC) chloride channel at 3.7 a resolution

Analyse Structure of calcium-bound MTMEM16A(AC) chloride channel at 3.7 a resolution in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7B5C
Type: protein
Length: 1,436 residues
Chains: 2
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Anoctamin-1
UniProt: Q8BHY3
Ligands: CA
Pockets: 20 · best druggability 0.83

Structure

electron microscopy · 1 distinct chain · 57% helix, 3% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Anoctamin-1	protein	718	57% helix, 3% strand	Q8BHY3

Ligands and binding sites

CA · Calcium ion · metal · 4 copies · chains A, B

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

Pockets

20 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	645	0.83	0.87	67	empty
2	1141	0.82	0.83	109	empty
3	1170	0.81	0.83	103	empty
4	683	0.81	0.85	72	empty
5	812	0.79	0.82	75	empty

Interfaces

1 interface between chains.

A–B · 1082 Å² buried · 4 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 8 disulfide (disulfide).

Compared structures

7B5C · Structure of calcium-bound mTMEM16A(ac) chloride channel at 3.7 A resolution · the same entry in another collection · chain A against A, TM-score 1.00
Q8BHY3 · AlphaFold monomer V2.0 prediction for anoctamin-1 (Q8BHY3) · a predicted model of the same protein · chain A against A, TM-score 0.97

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 Q8BHY3
Elsewhere: RCSB PDB 7B5C · PDBe 7B5C · UniProt Q8BHY3

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