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A complex between DISHEVELLED2 and clathrin adaptor ap-2

Analyse A complex between DISHEVELLED2 and clathrin adaptor ap-2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3ML6
Type: protein
Length: 2,054 residues
Chains: 6
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Chimeric complex between protein DISHEVELLED2 homolog dvl-2 and clathrin adaptor ap-2…
UniProt: Q60838, P84092
Pockets: 20 · best druggability 0.73

Structure

x-ray diffraction · 6 distinct chains · 11% helix, 47% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Chimeric complex between protein DISHEVELLED2 homolog dvl-2 and clathrin adaptor ap-2 complex subunit mu	protein	351	11% helix, 47% strand	Q60838, P84092
B	Chimeric complex between protein DISHEVELLED2 homolog dvl-2 and clathrin adaptor ap-2 complex subunit mu	protein	339	12% helix, 48% strand	Q60838, P84092
C	Chimeric complex between protein DISHEVELLED2 homolog dvl-2 and clathrin adaptor ap-2 complex subunit mu	protein	350	11% helix, 47% strand	Q60838, P84092
D	Chimeric complex between protein DISHEVELLED2 homolog dvl-2 and clathrin adaptor ap-2 complex subunit mu	protein	336	12% helix, 48% strand	Q60838, P84092
E	Chimeric complex between protein DISHEVELLED2 homolog dvl-2 and clathrin adaptor ap-2 complex subunit mu	protein	338	12% helix, 48% strand	Q60838, P84092
F	Chimeric complex between protein DISHEVELLED2 homolog dvl-2 and clathrin adaptor ap-2 complex subunit mu	protein	340	11% helix, 48% strand	Q60838, P84092

Pockets

20 pockets found on a 1 Å grid, 13 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	581	0.73	0.81	45	empty
2	263	0.59	0.79	31	empty
3	282	0.59	0.78	36	empty
4	235	0.57	0.78	36	empty
5	98	0.55	0.84	26	empty

Interfaces

6 interfaces between chains.

A–E · 1353 Å² buried · 22 hydrogen bonds · protein-protein
B–F · 1327 Å² buried · 18 hydrogen bonds · protein-protein
B–E · 578 Å² buried · 4 hydrogen bonds · protein-protein
A–F · 571 Å² buried · 4 hydrogen bonds · protein-protein
A–C · 548 Å² buried · 6 hydrogen bonds · protein-protein

Compared structures

3ML6 · a complex between Dishevelled2 and clathrin adaptor AP-2 · the same entry in another collection · chain C against C, 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 B against A, TM-score 0.67

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 Q60838
Every structure of UniProt P84092
Elsewhere: RCSB PDB 3ML6 · PDBe 3ML6 · UniProt Q60838 · UniProt P84092

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