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Crystal structure of an asymmetric dimer of the ubiquitin ligase HUWE1

Analyse Crystal structure of an asymmetric dimer of the ubiquitin ligase HUWE1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5LP8
Type: protein
Length: 848 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: E3 ubiquitin-protein ligase HUWE1
EC: 6.3.2.-
UniProt: Q7Z6Z7
Pockets: 10 · best druggability 0.80

Structure

x-ray diffraction · 2 distinct chains · 50% helix, 13% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
B	E3 ubiquitin-protein ligase HUWE1 (EC 6.3.2.-)	protein	416	51% helix, 14% strand	Q7Z6Z7
A	E3 ubiquitin-protein ligase HUWE1 (EC 6.3.2.-)	protein	432	50% helix, 13% strand	Q7Z6Z7

Pockets

10 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	183	0.80	0.95	28	empty
2	423	0.75	0.85	44	empty
3	321	0.71	0.84	40	empty
4	167	0.51	0.78	20	empty
5	104	0.43	0.78	23	empty

Interfaces

1 interface between chains.

B–A · 1371 Å² buried · 7 hydrogen bonds · protein-protein

Compared structures

5LP8 · Crystal structure of an asymmetric dimer of the ubiquitin ligase HUWE1 · the same entry in another collection · chain B against B, 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 Q7Z6Z7
Elsewhere: RCSB PDB 5LP8 · PDBe 5LP8 · UniProt Q7Z6Z7

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