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Structure of USP15 dusp-ubl deletion mutant

Analyse Structure of USP15 dusp-ubl deletion mutant in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4A3P
Type: protein
Length: 210 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Ubiquitin carboxyl-terminal hydrolase 15
EC: 3.4.19.12
UniProt: Q9Y4E8
Ligands: IOD
Pockets: 1 · best druggability 0.31

Structure

x-ray diffraction · 1 distinct chain · 26% helix, 30% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Ubiquitin carboxyl-terminal hydrolase 15 (EC 3.4.19.12)	protein	210	26% helix, 30% strand	Q9Y4E8

Ligands and binding sites

IOD · Iodide ion · ion · chains A
ACT · Acetate ion · additive · chains A

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

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	63	0.31	0.75	15	IOD

Compared structures

4A3P · Structure of USP15 DUSP-UBL deletion mutant · 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 0.75

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 4A3P · PDBe 4A3P · UniProt Q9Y4E8

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