MolNFT v1 · #149491 · protein

X-ray structure of NSD3-PWWP1 in complex with compound 3

6G24 · Histone-lysine N-methyltransferase NSD3: “X-ray structure of NSD3-PWWP1 in complex with compound 3”. X-ray diffraction, 1 ligand (EH2), 2 pockets (best druggability 0.36). MolNFT v1 #149491 on GenesisL1: 3D structure, binding sites…

PDB: 6G24
Type: protein
Length: 121 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Histone-lysine N-methyltransferase NSD3
EC: 2.1.1.43
UniProt: Q9BZ95
Ligands: EH2
Pockets: 2 · best druggability 0.36

Structure

x-ray diffraction · 1 distinct chain · 31% helix, 22% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Histone-lysine N-methyltransferase NSD3 (EC 2.1.1.43)	protein	121	31% helix, 22% strand	Q9BZ95

Ligands and binding sites

EH2 · 2-[(~{E})-2-thiophen-2-ylethenyl]benzoic acid · ligand · 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	78	0.36	0.76	12	empty
2	67	0.35	0.76	10	empty

Compared structures

6G24 · X-ray structure of NSD3-PWWP1 in complex with compound 3 · the same entry in another collection · chain A against A, TM-score 1.00
Q9BZ95 · AlphaFold monomer V2.0 prediction for histone-lysine N-methyltransferase NSD3 (Q9BZ95) · 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 Q9BZ95
Elsewhere: RCSB PDB 6G24 · PDBe 6G24 · UniProt Q9BZ95

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