MolNFT v1 · #102860 · protein

Crystal structure of the N-terminal domains of muskelin

4OYU: “Crystal structure of the N-terminal domains of muskelin”. X-ray diffraction, 2 pockets (best druggability 0.41). MolNFT v1 #102860 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 4OYU
Type: protein
Length: 357 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Muskelin
UniProt: Q99PV3
Pockets: 2 · best druggability 0.41

Structure

x-ray diffraction · 2 distinct chains · 19% helix, 39% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Muskelin	protein	178	19% helix, 39% strand	Q99PV3
B	Muskelin	protein	179	19% helix, 39% strand	Q99PV3

Ligands and binding sites

EDO · 1,2-ethanediol · additive · 23 copies · chains A, B
GOL · Glycerol · additive · chains A

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

Pockets

2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	117	0.41	0.76	19	empty
2	96	0.39	0.76	15	EDO

Interfaces

1 interface between chains.

A–B · 515 Å² buried · 6 hydrogen bonds · protein-protein

Compared structures

4OYU · Crystal structure of the N-terminal domains of muskelin · the same entry in another collection · chain A against A, TM-score 1.00
Q99PV3 · AlphaFold monomer V2.0 prediction for muskelin (Q99PV3) · 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 Q99PV3
Elsewhere: RCSB PDB 4OYU · PDBe 4OYU · UniProt Q99PV3

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.