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Crystal structure of the quaternary complex of histone H3-H4 heterodimer with chaperone ASF1 and the replicative helicase subunit MCM2

Analyse Crystal structure of the quaternary complex of histone H3-H4 heterodimer with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5C3I
Type: protein
Length: 2,198 residues
Chains: 24
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Histone chaperone ASF1A; Histone H3.1; Histone H4; DNA replication licensing factor…
EC: 3.6.4.12
UniProt: Q9Y294, P68431, P62805, P49736
Pockets: 20 · best druggability 0.81

Structure

x-ray diffraction · 16 distinct chains · 37% helix, 27% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, M	Histone chaperone ASF1A	protein	152	12% helix, 53% strand	Q9Y294
B	Histone H3.1	protein	87	71% helix, 5% strand	P68431
C, O, S	Histone H4	protein	78	64% helix, 10% strand	P62805
D	DNA replication licensing factor MCM2,MCM2 (EC 3.6.4.12)	protein	63	22% helix, 8% strand	P49736
E, I	Histone chaperone ASF1A	protein	153	10% helix, 55% strand	Q9Y294
F	Histone H3.1	protein	88	58% helix, 11% strand	P68431
G, W	Histone H4	protein	77	64% helix, 12% strand	P62805
H, L, X	DNA replication licensing factor MCM2,MCM2 (EC 3.6.4.12)	protein	56	34% helix, 9% strand	P49736
J	Histone H3.1	protein	84	62% helix, 11% strand	P68431
K	Histone H4	protein	76	63% helix, 9% strand	P62805
N, V	Histone H3.1	protein	76	67% helix, 5% strand	P68431
P	DNA replication licensing factor MCM2,MCM2 (EC 3.6.4.12)	protein	48	27% helix, 6% strand	P49736
Q	Histone chaperone ASF1A	protein	154	12% helix, 53% strand	Q9Y294
R	Histone H3.1	protein	74	70% helix, 4% strand	P68431
T	DNA replication licensing factor MCM2,MCM2 (EC 3.6.4.12)	protein	56	38% helix, 5% strand	P49736
U	Histone chaperone ASF1A	protein	150	12% helix, 57% strand	Q9Y294

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	1196	0.81	0.82	99	empty
2	757	0.78	0.82	95	empty
3	676	0.69	0.77	57	empty
4	480	0.65	0.78	46	empty
5	229	0.65	0.83	34	empty

Interfaces

69 interfaces between chains.

F–G · 2230 Å² buried · 16 hydrogen bonds · protein-protein
B–C · 2226 Å² buried · 18 hydrogen bonds · protein-protein
V–W · 2210 Å² buried · 16 hydrogen bonds · protein-protein
R–S · 2191 Å² buried · 13 hydrogen bonds · protein-protein
N–O · 2172 Å² buried · 17 hydrogen bonds · protein-protein

Compared structures

5C3I · Crystal structure of the quaternary complex of histone H3-H4 heterodimer with chaperone… · the same entry in another collection · chain J against J, 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 Q9Y294
Every structure of UniProt P68431
Every structure of UniProt P62805
Every structure of UniProt P49736
Elsewhere: RCSB PDB 5C3I · PDBe 5C3I · UniProt Q9Y294 · UniProt P68431 · UniProt P62805 · UniProt P49736

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