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NSD1-PHD_5-C5HCH tandem domain structure

Analyse NSD1-PHD_5-C5HCH tandem domain structure in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2NAA
Type: protein
Length: 94 residues
Chains: 1
Method: solution nmr
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Histone-lysine N-methyltransferase, H3 lysine-36 and H4 lysine-20 specific
EC: 2.1.1.43
UniProt: O88491
Ligands: ZN

Structure

solution nmr · 1 distinct chain · 3% helix, 20% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Histone-lysine N-methyltransferase, H3 lysine-36 and H4 lysine-20 specific (EC 2.1.1.43)	protein	94	3% helix, 20% strand	O88491

Ligands and binding sites

ZN · Zinc ion · metal · 4 copies · chains A

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

Compared structures

2NAA · NSD1-PHD_5-C5HCH tandem domain structure · the same entry in another collection · chain A against A, TM-score 1.00
O88491 · AlphaFold monomer V2.0 prediction for histone-lysine N-methyltransferase, H3 lysine-36… · a predicted model of the same protein · chain A against A, TM-score 0.86

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 O88491
Elsewhere: RCSB PDB 2NAA · PDBe 2NAA · UniProt O88491

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