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Structure of the dusp-ubl domains of USP15

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

PDB: 3PPA
Type: protein
Length: 209 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: SO4

Structure

x-ray diffraction · 1 distinct chain · 21% helix, 24% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Ubiquitin carboxyl-terminal hydrolase 15 (EC 3.4.19.12)	protein	209	21% helix, 24% strand	Q9Y4E8

Ligands and binding sites

SO4 · Sulfate ion · ion · 3 copies · chains A
CIT · Citric acid · additive · chains A

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

Compared structures

3PPA · Structure of the Dusp-Ubl domains of Usp15 · 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 0.59

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 3PPA · PDBe 3PPA · UniProt Q9Y4E8

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