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Structure of deubiquitinase

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

PDB: 6KBE
Type: protein
Length: 389 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Ubiquitin thioesterase; Polyubiquitin-C
EC: 3.4.19.12
UniProt: B9G207, P0CG48
Pockets: 4 · best druggability 0.59

Structure

x-ray diffraction · 2 distinct chains · 43% helix, 23% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
B	Ubiquitin thioesterase (EC 3.4.19.12)	protein	239	56% helix, 16% strand	B9G207
G	Polyubiquitin-C	protein	150	22% helix, 35% strand	P0CG48

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	209	0.59	0.81	31	empty
2	124	0.50	0.80	18	empty
3	84	0.39	0.78	16	empty
4	87	0.37	0.76	17	empty

Interfaces

1 interface between chains.

B–G · 1823 Å² buried · 39 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 1 d-amino (D-amino acid).

Compared structures

6KBE · Structure of Deubiquitinase · 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 B9G207
Every structure of UniProt P0CG48
Elsewhere: RCSB PDB 6KBE · PDBe 6KBE · UniProt B9G207 · UniProt P0CG48

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