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The enth domain from epsin-2 in complex with phosphatidylinositol 4,5- bisphosphate (PIP2)

Analyse The enth domain from epsin-2 in complex with phosphatidylinositol 4,5… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5OO7
Type: protein
Length: 513 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: SLA2
UniProt: G0S106
Pockets: 6 · best druggability 0.77

Structure

x-ray diffraction · 2 distinct chains · 72% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	SLA2	protein	257	74% helix, 0% strand	G0S106
B	SLA2	protein	256	70% helix, 0% strand	G0S106

Ligands and binding sites

GOL · Glycerol · additive · chains B

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

Pockets

6 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	691	0.77	0.82	64	empty
2	220	0.55	0.78	29	empty
3	192	0.49	0.76	27	empty
4	153	0.46	0.76	27	empty
5	81	0.40	0.78	14	GOL

Interfaces

1 interface between chains.

A–B · 923 Å² buried · 15 hydrogen bonds · protein-protein

Compared structures

5OO7 · The ENTH domain from epsin-2 in complex with phosphatidylinositol 4,5-bisphosphate (PIP2) · 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 G0S106
Elsewhere: RCSB PDB 5OO7 · PDBe 5OO7 · UniProt G0S106

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