MolNFT v1 · #152232 · protein

The ferm domain of human EPB41L3

6IBE · Band 4.1-like protein 3: “The ferm domain of human EPB41L3”. X-ray diffraction, 3 pockets (best druggability 0.70). MolNFT v1 #152232 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 6IBE
Type: protein
Length: 284 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Band 4.1-like protein 3
UniProt: Q9Y2J2
Pockets: 3 · best druggability 0.70

Structure

x-ray diffraction · 1 distinct chain · 35% helix, 26% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Band 4.1-like protein 3	protein	284	35% helix, 26% strand	Q9Y2J2

Ligands and binding sites

EDO · 1,2-ethanediol · additive · 6 copies · chains A
MES · 2-(N-morpholino)-ethanesulfonic acid · additive · 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, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	443	0.70	0.81	46	EDO
2	176	0.54	0.79	28	empty
3	59	0.30	0.75	15	empty

Compared structures

6IBE · The FERM domain of Human EPB41L3 · the same entry in another collection · chain A against A, TM-score 1.00
Q9Y2J2 · AlphaFold monomer V2.0 prediction for band 4.1-like protein 3 (Q9Y2J2) · a predicted model of the same protein · chain A against A, TM-score 0.97

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 Q9Y2J2
Elsewhere: RCSB PDB 6IBE · PDBe 6IBE · UniProt Q9Y2J2

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