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Crystal structure of PELLINO2 fha domain at 1.8 ångströms resolution

Analyse Crystal structure of PELLINO2 fha domain at 1.8 ångströms resolution in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3EGA
Type: protein
Length: 219 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Protein pellino homolog 2
UniProt: Q9HAT8
Ligands: SO4
Pockets: 3 · best druggability 0.53

Structure

x-ray diffraction · 1 distinct chain · 0% helix, 42% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Protein pellino homolog 2	protein	219	0% helix, 42% strand	Q9HAT8

Ligands and binding sites

SO4 · Sulfate ion · ion · chains A

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

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	213	0.53	0.77	33	empty
2	130	0.42	0.75	30	empty
3	61	0.29	0.75	21	empty

Modifications

Observed in the structure: 5 modified (engineered).

Compared structures

3EGA · Crystal structure of Pellino2 FHA Domain at 1.8 Angstroms resolution · the same entry in another collection · chain A against A, TM-score 1.00
Q9HAT8 · AlphaFold monomer V2.0 prediction for E3 ubiquitin-protein ligase pellino homolog 2… · a predicted model of the same protein · chain A against A, TM-score 0.94

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 Q9HAT8
Elsewhere: RCSB PDB 3EGA · PDBe 3EGA · UniProt Q9HAT8

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