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MU2 adaptin subunit (AP50) of AP2 adaptor (second domain), complexed with TGN38 internalization peptide dyqrln

Analyse MU2 adaptin subunit (AP50) of AP2 adaptor (second domain), complexed with TGN38… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1BXX
Type: protein
Length: 262 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Protein (AP50); Protein (TGN38 peptide)
UniProt: P84092
Pockets: 2 · best druggability 0.41

Structure

x-ray diffraction · 2 distinct chains · 1% helix, 55% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Protein (AP50)	protein	256	1% helix, 55% strand	P84092
P	Protein (TGN38 peptide)	protein	6	0% helix, 33% strand	—

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	118	0.41	0.76	19	empty
2	116	0.39	0.74	25	empty

Interfaces

1 interface between chains.

A–P · 456 Å² buried · 9 hydrogen bonds · protein-protein

Compared structures

1BXX · MU2 adaptin subunit (AP50) of AP2 adaptor (second domain), complexed with TGN38… · the same entry in another collection · chain A against A, TM-score 1.00
P84092 · AlphaFold monomer V2.0 prediction for ap-2 complex subunit mu (P84092) · a predicted model of the same protein · chain A against A, TM-score 0.95

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 P84092
Elsewhere: RCSB PDB 1BXX · PDBe 1BXX · UniProt P84092

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