MolNFT v1 · #62464 · protein

Structure of PELLINO2 fha domain at 3.3 ångströms resolution.

3EGB · Protein pellino homolog 2: “Structure of PELLINO2 fha domain at 3.3 ångströms resolution.”. X-ray diffraction, 8 pockets (best druggability 0.73). MolNFT v1 #62464 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 3EGB
Type: protein
Length: 458 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Protein pellino homolog 2
UniProt: Q9HAT8
Pockets: 8 · best druggability 0.73

Structure

x-ray diffraction · 2 distinct chains · 6% helix, 40% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Protein pellino homolog 2	protein	235	7% helix, 39% strand	Q9HAT8
B	Protein pellino homolog 2	protein	223	5% helix, 40% strand	Q9HAT8

Pockets

8 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	817	0.73	0.78	89	empty
2	143	0.50	0.79	27	empty
3	116	0.45	0.78	29	empty
4	161	0.44	0.75	29	empty
5	123	0.44	0.77	25	empty

Interfaces

1 interface between chains.

A–B · 507 Å² buried · 11 hydrogen bonds · protein-protein

Compared structures

3EGB · Structure of Pellino2 FHA domain at 3.3 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 B against A, TM-score 0.95

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 3EGB · PDBe 3EGB · UniProt Q9HAT8

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