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Crystal structure of bar-pH domain of APPL1

Analyse Crystal structure of bar-pH domain of APPL1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2Q13
Type: protein
Length: 364 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Dcc-interacting protein 13 alpha
UniProt: Q9UKG1
Pockets: 1 · best druggability 0.27

Structure

x-ray diffraction · 1 distinct chain · 66% helix, 10% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Dcc-interacting protein 13 alpha	protein	364	66% helix, 10% strand	Q9UKG1

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	56	0.27	0.74	15	empty

Compared structures

2Q13 · Crystal structure of BAR-PH domain of APPL1 · the same entry in another collection · chain A against A, TM-score 1.00
Q9UKG1 · AlphaFold monomer V2.0 prediction for dcc-interacting protein 13-alpha (Q9UKG1) · a predicted model of the same protein · chain A against A, TM-score 0.94

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 Q9UKG1
Elsewhere: RCSB PDB 2Q13 · PDBe 2Q13 · UniProt Q9UKG1

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