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Crystal structure of the human USP11 dusp-ubl domains

Analyse Crystal structure of the human USP11 dusp-ubl domains in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4MEL
Type: protein
Length: 426 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Ubiquitin carboxyl-terminal hydrolase 11
EC: 3.4.19.12
UniProt: P51784
Pockets: 3 · best druggability 0.39

Structure

x-ray diffraction · 1 distinct chain · 22% helix, 26% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Ubiquitin carboxyl-terminal hydrolase 11 (EC 3.4.19.12)	protein	213	22% helix, 26% strand	P51784

Pockets

3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	84	0.39	0.77	22	empty
2	55	0.32	0.76	16	empty
3	62	0.27	0.73	10	empty

Interfaces

1 interface between chains.

A–B · 1567 Å² buried · 23 hydrogen bonds · protein-protein

Compared structures

4MEL · Crystal Structure of the human USP11 DUSP-UBL domains · the same entry in another collection · chain A against A, TM-score 1.00
P51784 · AlphaFold monomer V2.0 prediction for ubiquitin carboxyl-terminal hydrolase 11 (P51784) · a predicted model of the same protein · chain A against A, TM-score 0.52

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 P51784
Elsewhere: RCSB PDB 4MEL · PDBe 4MEL · UniProt P51784

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