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Mechanism of USP7 (hausp) activation by its C-terminal ubiquitin-like domain (hubl) and allosteric regulation by gmp-synthetase.

Analyse Mechanism of USP7 (hausp) activation by its C-terminal ubiquitin-like domain… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2YLM
Type: protein
Length: 529 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Ubiquitin carboxyl-terminal hydrolase 7
EC: 3.4.19.12
UniProt: Q93009
Ligands: CL
Pockets: 5 · best druggability 0.60

Structure

x-ray diffraction · 1 distinct chain · 23% helix, 32% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Ubiquitin carboxyl-terminal hydrolase 7 (EC 3.4.19.12)	protein	529	23% helix, 32% strand	Q93009

Ligands and binding sites

CL · Chloride ion · ion · chains A

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

Pockets

5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	218	0.60	0.81	25	empty
2	293	0.52	0.74	42	empty
3	101	0.45	0.79	15	empty
4	54	0.30	0.75	11	empty
5	65	0.28	0.73	16	empty

Compared structures

2YLM · Mechanism of USP7 (HAUSP) activation by its C-terminal ubiquitin-like domain (HUBL) and… · 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 Q93009
Elsewhere: RCSB PDB 2YLM · PDBe 2YLM · UniProt Q93009

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