MolNFT v1 · #15155 · protein

Structure of the set domain histone lysine methyltransferase CLR4

1MVX · Cryptic loci regulator 4: “Structure of the set domain histone lysine methyltransferase CLR4”. X-ray diffraction, 3 ligands (ZN, NI, SO4), 3 pockets (best druggability 0.62). MolNFT v1 #15155 on GenesisL1: 3D structure, binding…

PDB: 1MVX
Type: protein
Length: 269 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cryptic loci regulator 4
UniProt: O60016
Ligands: ZN, NI, SO4
Pockets: 3 · best druggability 0.62

Structure

x-ray diffraction · 1 distinct chain · 14% helix, 22% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Cryptic loci regulator 4	protein	269	14% helix, 22% strand	O60016

Ligands and binding sites

ZN · Zinc ion · metal · 3 copies · chains A
NI · Nickel (II) ion · metal · chains A
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, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	337	0.62	0.78	39	SO4
2	114	0.56	0.84	19	empty
3	153	0.45	0.76	25	empty

Compared structures

1MVX · structure of the SET domain histone lysine methyltransferase Clr4 · the same entry in another collection · chain A against A, TM-score 1.00
O60016 · AlphaFold monomer V2.0 prediction for histone-lysine N-methyltransferase, H3 lysine-9… · a predicted model of the same protein · chain A 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 O60016
Elsewhere: RCSB PDB 1MVX · PDBe 1MVX · UniProt O60016

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