MolNFT v1 · #149369 · protein

Disulfide between ubiquitin G76C and the E3 hect ligase HUWE1

6FYH · E3 ubiquitin-protein ligase HUWE1: “Disulfide between ubiquitin G76C and the E3 hect ligase HUWE1”. X-ray diffraction, 2 ligands (ZN, SO4), 2 pockets (best druggability 0.32). MolNFT v1 #149369 on GenesisL1: 3D structure, binding…

PDB: 6FYH
Type: protein
Length: 191 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: E3 ubiquitin-protein ligase HUWE1; Polyubiquitin-B
EC: 2.3.2.26
UniProt: Q7Z6Z7, P0CG47
Ligands: ZN, SO4
Pockets: 2 · best druggability 0.32

Structure

x-ray diffraction · 2 distinct chains · 30% helix, 23% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	E3 ubiquitin-protein ligase HUWE1 (EC 2.3.2.26)	protein	115	37% helix, 17% strand	Q7Z6Z7
B	Polyubiquitin-B	protein	76	20% helix, 33% strand	P0CG47

Ligands and binding sites

ZN · Zinc ion · metal · 6 copies · chains A, B
SO4 · Sulfate ion · ion · 2 copies · chains A

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

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	50	0.32	0.77	15	empty
2	52	0.27	0.73	10	empty

Interfaces

1 interface between chains.

A–B · 587 Å² buried · 11 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

6FYH · Disulfide between ubiquitin G76C and the E3 HECT ligase Huwe1 · the same entry in another collection · chain A against A, 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
Every structure of UniProt P0CG47
Elsewhere: RCSB PDB 6FYH · PDBe 6FYH · UniProt Q7Z6Z7 · UniProt P0CG47

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