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Structure of the endocytic adaptor complex aenth

Analyse Structure of the endocytic adaptor complex aenth in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7B2L
Type: protein
Length: 3,152 residues
Chains: 16
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Enth domain of epsin ENT1; Anth domain of SLA2
UniProt: Q12518, P33338
Ligands: PIO
Pockets: 20 · best druggability 0.73

Structure

electron microscopy · 2 distinct chains · 74% helix, 1% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, C, F, H, K, M, P, R	Enth domain of epsin ENT1	protein	147	72% helix, 1% strand	Q12518
B, D, G, I, L, N, Q, S	Anth domain of SLA2	protein	247	74% helix, 0% strand	P33338

Ligands and binding sites

PIO · [(2R)-2-octanoyloxy-3-[oxidanyl-[(1R,2R,3S,4R,5R,6S)-2, 3,6-tris(oxidanyl)-4,5-diphosphonooxy-cyclohexyl]oxy-phosphoryl]oxy-propyl] octanoate · ligand · 20 copies · chains A, C, B, D, F, H, G, I, K, M, L, N, P, R, Q, S

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

Pockets

20 pockets found on a 1 Å grid, 18 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	896	0.73	0.78	83	PIO
2	1188	0.72	0.76	79	empty
3	1197	0.72	0.75	90	empty
4	412	0.70	0.81	51	empty
5	425	0.70	0.81	48	empty

Interfaces

32 interfaces between chains.

C–D · 880 Å² buried · 10 hydrogen bonds · protein-protein
M–N · 880 Å² buried · 10 hydrogen bonds · protein-protein
H–I · 878 Å² buried · 10 hydrogen bonds · protein-protein
R–S · 878 Å² buried · 10 hydrogen bonds · protein-protein
A–B · 785 Å² buried · 4 hydrogen bonds · protein-protein

Compared structures

7B2L · Structure of the endocytic adaptor complex AENTH · the same entry in another collection · chain L against L, 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 Q12518
Every structure of UniProt P33338
Elsewhere: RCSB PDB 7B2L · PDBe 7B2L · UniProt Q12518 · UniProt P33338

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