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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: 5J9T
Type: protein
Length: 2,220 residues
Chains: 12
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 0.79

Structure

x-ray diffraction · 9 distinct chains · 54% helix, 8% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
E, A	Histone acetyltransferase ESA1 (EC 2.3.1.48)	protein	278	37% helix, 23% strand	Q08649
F	Chromatin modification-related protein EAF6	protein	68	72% helix, 0% strand	P47128
G	Enhancer of polycomb-like protein 1	protein	273	55% helix, 1% strand	P43572
H, D, L	Chromatin modification-related protein YNG2	protein	119	84% helix, 0% strand	P38806
B	Chromatin modification-related protein EAF6	protein	77	69% helix, 3% strand	P47128
C	Enhancer of polycomb-like protein 1	protein	268	58% helix, 1% strand	P43572
I	Histone acetyltransferase ESA1 (EC 2.3.1.48)	protein	277	36% helix, 23% strand	Q08649
J	Chromatin modification-related protein EAF6	protein	75	69% helix, 3% strand	P47128
K	Enhancer of polycomb-like protein 1	protein	269	56% helix, 1% strand	P43572

Pockets

20 pockets found on a 1 Å grid, 14 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	840	0.79	0.82	68	empty
2	798	0.79	0.82	66	empty
3	683	0.78	0.83	68	empty
4	778	0.78	0.82	61	empty
5	787	0.78	0.81	76	empty

Interfaces

23 interfaces between chains.

K–L · 2999 Å² buried · 34 hydrogen bonds · protein-protein
G–H · 2958 Å² buried · 30 hydrogen bonds · protein-protein
I–K · 2947 Å² buried · 51 hydrogen bonds · protein-protein
C–D · 2931 Å² buried · 33 hydrogen bonds · protein-protein
E–G · 2928 Å² buried · 55 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 3 modified (acetylation).

Compared structures

5J9T · Crystal structure of the NuA4 core complex · the same entry in another collection · chain L against L, 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 5J9T · PDBe 5J9T · UniProt Q08649 · UniProt P47128 · UniProt P43572 · UniProt P38806

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