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Solution structure of the dusp domain of HUSP15

Analyse Solution structure of the dusp domain of HUSP15 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1W6V
Type: protein
Length: 120 residues
Chains: 1
Method: solution nmr
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Ubiquitin carboxyl-terminal hydrolase 15
EC: 3.1.2.15
UniProt: Q9Y4E8
Pockets: 1 · best druggability 0.39

Structure

solution nmr · 1 distinct chain · 28% helix, 14% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Ubiquitin carboxyl-terminal hydrolase 15 (EC 3.1.2.15)	protein	120	28% helix, 14% strand	Q9Y4E8

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	96	0.39	0.76	16	empty

Compared structures

1W6V · Solution structure of the DUSP domain of hUSP15 · the same entry in another collection · chain A against A, TM-score 1.00
Q9Y4E8 · AlphaFold monomer V2.0 prediction for ubiquitin carboxyl-terminal hydrolase 15 (Q9Y4E8) · a predicted model of the same protein · chain A against A, TM-score 0.92

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 Q9Y4E8
Elsewhere: RCSB PDB 1W6V · PDBe 1W6V · UniProt Q9Y4E8

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