Research workbench

Human mof K274P crystal structure

Analyse Human mof K274P crystal structure in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5J8F
Type: protein
Length: 265 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, CL
Pockets: 3 · best druggability 0.64

Structure

x-ray diffraction · 1 distinct chain · 35% helix, 23% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Histone acetyltransferase KAT8 (EC 2.3.1.48)	protein	265	35% helix, 23% strand	Q9H7Z6

Ligands and binding sites

ZN · Zinc ion · metal · chains A
CL · Chloride ion · ion · 2 copies · chains A

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

Pockets

3 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	202	0.64	0.84	41	CL
2	83	0.41	0.78	17	empty
3	71	0.38	0.78	16	empty

Compared structures

5J8F · Human MOF K274P crystal structure · 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 0.98

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 5J8F · PDBe 5J8F · UniProt Q9H7Z6

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