MolNFT v1 · #43263 · protein

ASHH2 a cw domain

2L7P · Histone-lysine N-methyltransferase ASHH2: “ASHH2 a cw domain”. Solution nmr, 1 ligand (ZN). MolNFT v1 #43263 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 2L7P
Type: protein
Length: 100 residues
Chains: 1
Method: solution nmr
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Histone-lysine N-methyltransferase ASHH2
EC: 2.1.1.43
UniProt: Q2LAE1
Ligands: ZN

Structure

solution nmr · 1 distinct chain · 15% helix, 8% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Histone-lysine N-methyltransferase ASHH2 (EC 2.1.1.43)	protein	100	15% helix, 8% strand	Q2LAE1

Ligands and binding sites

ZN · Zinc ion · metal · chains A

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

Compared structures

2L7P · ASHH2 a CW domain · the same entry in another collection · chain A against A, TM-score 1.00
Q2LAE1 · AlphaFold monomer V2.0 prediction for histone-lysine N-methyltransferase ASHH2 (Q2LAE1) · a predicted model of the same protein · chain A against A, TM-score 0.54

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 Q2LAE1
Elsewhere: RCSB PDB 2L7P · PDBe 2L7P · UniProt Q2LAE1

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