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ASH1L set domain in complex with as-85

Analyse ASH1L set domain in complex with as-85 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6WZW
Type: protein
Length: 221 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Histone-lysine N-methyltransferase ASH1L
EC: 2.1.1.-, 2.1.1.359
UniProt: Q9NR48
Ligands: SAM, UG7, ZN
Pockets: 1 · best druggability 0.66

Structure

x-ray diffraction · 1 distinct chain · 12% helix, 29% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Histone-lysine N-methyltransferase ASH1L (EC 2.1.1.-, 2.1.1.359)	protein	221	12% helix, 29% strand	Q9NR48

Ligands and binding sites

SAM · S-adenosylmethionine · ligand · chains A
UG7 · N-{[3-(3-carbamothioylphenyl)-1-{1-[(trifluoromethyl) sulfonyl]piperidin-4-yl}-1H-indol-6-yl]methyl}azetidine-3-carboxamide · ligand · chains A
ZN · Zinc ion · metal · 3 copies · chains A
EPE · 4-(2-hydroxyethyl)-1-piperazine ethanesulfonic acid · additive · chains A

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

Pockets

1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	217	0.66	0.84	37	SAM, UG7

Compared structures

6WZW · Ash1L SET domain in complex with AS-85 · 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 Q9NR48
Elsewhere: RCSB PDB 6WZW · PDBe 6WZW · UniProt Q9NR48

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