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Conformational Flexibility Underlies Ubiquitin Ligation Mediated by the WWP1 HECT domain E3 Ligase

Analyse Conformational Flexibility Underlies Ubiquitin Ligation Mediated by the WWP1… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1ND7
Type: protein
Length: 374 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 2.1
Source: Homo sapiens
Molecule: WW domain-containing protein 1
UniProt: Q9H0M0
Pockets: 3 · best druggability 0.79

Structure

x-ray diffraction · resolution 2.1 · 1 distinct chain · 49% helix, 11% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	WW domain-containing protein 1	protein	374	49% helix, 11% strand	Q9H0M0

Pockets

3 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	711	0.79	0.84	80	empty
2	70	0.36	0.77	20	empty
3	105	0.35	0.74	18	empty

Compared structures

1ND7 · Conformational flexibility underlies ubiquitin ligation mediated by the WWP1 hect domain… · the same entry in another collection · chain A against A, TM-score 1.00
Q9H0M0 · AlphaFold monomer V2.0 prediction for NEDD4-like E3 ubiquitin-protein ligase WWP1 (Q9H0M0) · a predicted model of the same protein · chain A against A, TM-score 0.96

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 Q9H0M0
Elsewhere: RCSB PDB 1ND7 · PDBe 1ND7 · UniProt Q9H0M0

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