Research workbench

Crystal structure of the NUA4 core complex

Analyse Crystal structure of the NUA4 core complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5J9Q
Type: protein
Length: 2,356 residues
Chains: 15
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Histone acetyltransferase ESA1; Chromatin modification-related protein EAF6; Enhancer of…
EC: 2.3.1.48
UniProt: Q08649, P47128, P43572, P38806
Pockets: 20 · best druggability 0.83

Structure

x-ray diffraction · 12 distinct chains · 48% helix, 9% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
E	Histone acetyltransferase ESA1 (EC 2.3.1.48)	protein	293	34% helix, 21% strand	Q08649
F	Chromatin modification-related protein EAF6	protein	75	64% helix, 0% strand	P47128
G	Enhancer of polycomb-like protein 1	protein	295	48% helix, 4% strand	P43572
A, I	Histone acetyltransferase ESA1 (EC 2.3.1.48)	protein	292	32% helix, 21% strand	Q08649
N	Enhancer of polycomb-like protein 1	protein	289	50% helix, 5% strand	P43572
C	Enhancer of polycomb-like protein 1	protein	293	50% helix, 5% strand	P43572
D, H, K	Chromatin modification-related protein YNG2	protein	120	84% helix, 0% strand	P38806
B	Chromatin modification-related protein EAF6	protein	79	66% helix, 3% strand	P47128
J	Chromatin modification-related protein EAF6	protein	76	63% helix, 0% strand	P47128
L	HTZ1	protein	5	0% helix, 20% strand	—
M	HTZ1	protein	4	0% helix, 25% strand	—
O	HTZ1	protein	3	0% helix, 0% strand	—

Pockets

20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	928	0.83	0.84	91	empty
2	1111	0.81	0.83	125	empty
3	986	0.80	0.82	99	empty
4	720	0.79	0.83	83	empty
5	1171	0.79	0.80	113	empty

Interfaces

41 interfaces between chains.

E–G · 4125 Å² buried · 68 hydrogen bonds · protein-protein
A–C · 3989 Å² buried · 67 hydrogen bonds · protein-protein
I–N · 3950 Å² buried · 64 hydrogen bonds · protein-protein
N–K · 2974 Å² buried · 28 hydrogen bonds · protein-protein
G–H · 2953 Å² buried · 29 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 3 modified (acetylation).

Compared structures

5J9Q · Crystal structure of the NuA4 core complex · the same entry in another collection · chain H against H, TM-score 1.00

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 Q08649
Every structure of UniProt P47128
Every structure of UniProt P43572
Every structure of UniProt P38806
Elsewhere: RCSB PDB 5J9Q · PDBe 5J9Q · UniProt Q08649 · UniProt P47128 · UniProt P43572 · UniProt P38806

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.