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Crystal structure of histone methyltransferase SET7/9 in complex with aam-1

Analyse Crystal structure of histone methyltransferase SET7/9 in complex with aam-1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3VUZ
Type: protein
Length: 246 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Histone-lysine N-methyltransferase SETD7
EC: 2.1.1.43
UniProt: Q8WTS6
Ligands: K15
Pockets: 1 · best druggability 0.55

Structure

x-ray diffraction · 1 distinct chain · 10% helix, 38% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Histone-lysine N-methyltransferase SETD7 (EC 2.1.1.43)	protein	246	10% helix, 38% strand	Q8WTS6

Ligands and binding sites

K15 · 5'-{[(3S)-3-amino-3-carboxypropyl](hexyl)amino}-5'-deoxyadenosine · ligand · 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	237	0.55	0.77	35	K15

Compared structures

3VUZ · Crystal structure of histone methyltransferase SET7/9 in complex with AAM-1 · the same entry in another collection · chain A against A, TM-score 1.00
Q8WTS6 · AlphaFold monomer V2.0 prediction for histone-lysine N-methyltransferase SETD7 (Q8WTS6) · a predicted model of the same protein · chain A against A, TM-score 0.96

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 Q8WTS6
Elsewhere: RCSB PDB 3VUZ · PDBe 3VUZ · UniProt Q8WTS6

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