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The crystal structure of human MYST1 from biortus.

Analyse The crystal structure of human MYST1 from biortus. in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7CMR
Type: protein
Length: 263 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Histone acetyltransferase KAT8
EC: 2.3.1.48
UniProt: Q9H7Z6
Ligands: ZN
Pockets: 2 · best druggability 0.68

Structure

x-ray diffraction · 1 distinct chain · 35% helix, 25% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Histone acetyltransferase KAT8 (EC 2.3.1.48)	protein	263	35% helix, 25% strand	Q9H7Z6

Ligands and binding sites

ZN · Zinc ion · metal · chains A
GOL · Glycerol · additive · 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, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	206	0.68	0.85	37	GOL
2	68	0.38	0.78	16	empty

Modifications

Observed in the structure: 1 modified (acetylation).

Compared structures

7CMR · The Crystal Structure of human MYST1 from Biortus. · the same entry in another collection · chain A against A, TM-score 1.00
Q9H7Z6 · AlphaFold monomer V2.0 prediction for histone acetyltransferase KAT8 (Q9H7Z6) · a predicted model of the same protein · chain A against A, TM-score 0.99

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 Q9H7Z6
Elsewhere: RCSB PDB 7CMR · PDBe 7CMR · UniProt Q9H7Z6

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