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Crystal structure of USP7/HAUSP in complex with ICP0

Analyse Crystal structure of USP7/HAUSP in complex with ICP0 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5C56
Type: protein
Length: 541 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Ubiquitin E3 ligase ICP0; Ubiquitin carboxyl-terminal hydrolase 7
EC: 3.4.19.12
UniProt: D3YPC2, Q93009
Pockets: 8 · best druggability 0.59

Structure

x-ray diffraction · 2 distinct chains · 22% helix, 33% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
B	Ubiquitin E3 ligase ICP0	protein	13	0% helix, 0% strand	D3YPC2
A	Ubiquitin carboxyl-terminal hydrolase 7 (EC 3.4.19.12)	protein	528	23% helix, 34% strand	Q93009

Pockets

8 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	226	0.59	0.80	26	empty
2	307	0.56	0.76	41	empty
3	160	0.44	0.75	17	empty
4	98	0.33	0.73	25	empty
5	57	0.31	0.76	16	empty

Interfaces

1 interface between chains.

B–A · 819 Å² buried · 16 hydrogen bonds · protein-protein

Compared structures

5C56 · Crystal structure of USP7/HAUSP in complex with ICP0 · the same entry in another collection · chain B against B, 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 D3YPC2
Every structure of UniProt Q93009
Elsewhere: RCSB PDB 5C56 · PDBe 5C56 · UniProt D3YPC2 · UniProt Q93009

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