Research workbench

ATTPC1 D454N with 1 mm edta state I

Analyse ATTPC1 D454N with 1 mm edta state I in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7TDF
Type: protein
Length: 1,188 residues
Chains: 2
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Two pore calcium channel protein 1
UniProt: Q94KI8
Pockets: 20 · best druggability 0.87

Structure

electron microscopy · 1 distinct chain · 75% helix, 1% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Two pore calcium channel protein 1	protein	594	75% helix, 1% strand	Q94KI8

Pockets

20 pockets found on a 1 Å grid, 11 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	846	0.87	0.89	44	empty
2	1195	0.77	0.78	83	empty
3	622	0.75	0.81	46	empty
4	364	0.67	0.80	36	empty
5	660	0.67	0.76	59	empty

Interfaces

1 interface between chains.

A–B · 3836 Å² buried · 14 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 disulfide (disulfide).

Compared structures

7TDF · AtTPC1 D454N with 1 mM EDTA state I · the same entry in another collection · chain A against A, TM-score 1.00
Q94KI8 · AlphaFold monomer V2.0 prediction for two pore calcium channel protein 1 (Q94KI8) · a predicted model of the same protein · chain A against A, TM-score 0.96

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 Q94KI8
Elsewhere: RCSB PDB 7TDF · PDBe 7TDF · UniProt Q94KI8

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