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Structure of moz

Analyse Structure of moz in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2LN0
Type: protein
Length: 110 residues
Chains: 1
Method: solution nmr
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Histone acetyltransferase KAT6A
EC: 2.3.1.48
UniProt: Q92794
Ligands: ZN

Structure

solution nmr · 1 distinct chain · 10% helix, 6% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Histone acetyltransferase KAT6A (EC 2.3.1.48)	protein	110	10% helix, 6% strand	Q92794

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

2LN0 · Structure of MOZ · the same entry in another collection · chain A against A, TM-score 1.00
Q92794 · AlphaFold monomer V2.0 prediction for histone acetyltransferase KAT6A (Q92794) · a predicted model of the same protein · chain A against A, TM-score 0.87

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 Q92794
Elsewhere: RCSB PDB 2LN0 · PDBe 2LN0 · UniProt Q92794

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