Research workbench

Crystal structure of cardiac specific histone methyltransferase SMYD1

Analyse Crystal structure of cardiac specific histone methyltransferase SMYD1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3N71
Type: protein
Length: 468 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Histone lysine methyltransferase SMYD1
UniProt: Q6DFW7
Ligands: SFG, ZN
Pockets: 2 · best druggability 0.77

Structure

x-ray diffraction · 1 distinct chain · 51% helix, 13% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Histone lysine methyltransferase SMYD1	protein	468	51% helix, 13% strand	Q6DFW7

Ligands and binding sites

SFG · Sinefungin · ligand · chains A
ZN · Zinc ion · metal · 3 copies · chains A
GOL · Glycerol · additive · 2 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

2 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	1006	0.77	0.79	106	SFG
2	372	0.68	0.81	48	empty

Compared structures

3N71 · Crystal structure of cardiac specific histone methyltransferase SmyD1 · 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 Q6DFW7
Elsewhere: RCSB PDB 3N71 · PDBe 3N71 · UniProt Q6DFW7

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