MolNFT v1 · #156390 · protein

A role for histone chaperone OSCHZ1 in histone recognition and deposition

6M2M · Probable histone H2A.3: “A role for histone chaperone OSCHZ1 in histone recognition and deposition”. X-ray diffraction, 13 pockets (best druggability 0.76). MolNFT v1 #156390 on GenesisL1: 3D structure, binding sites and pockets in…

PDB: 6M2M
Type: protein
Length: 1,068 residues
Chains: 15
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Probable histone H2A.3; Histone H2B.1; Expressed protein
UniProt: O81826, Q9LQQ4, Q2R2Z3
Pockets: 13 · best druggability 0.76

Structure

x-ray diffraction · 11 distinct chains · 68% helix, 3% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
E, A, C	Probable histone H2A.3	protein	88	68% helix, 5% strand	O81826
D	Histone H2B.1	protein	88	80% helix, 2% strand	Q9LQQ4
G	Probable histone H2A.3	protein	79	65% helix, 3% strand	O81826
I	Probable histone H2A.3	protein	80	66% helix, 4% strand	O81826
K	Probable histone H2A.3	protein	81	63% helix, 2% strand	O81826
F, B	Histone H2B.1	protein	86	74% helix, 5% strand	Q9LQQ4
J, L	Histone H2B.1	protein	89	74% helix, 3% strand	Q9LQQ4
H	Histone H2B.1	protein	88	72% helix, 5% strand	Q9LQQ4
M	Expressed protein	protein	10	30% helix, 0% strand	Q2R2Z3
N	Expressed protein	protein	15	0% helix, 0% strand	Q2R2Z3
O	Expressed protein	protein	13	23% helix, 0% strand	Q2R2Z3

Ligands and binding sites

GOL · Glycerol · additive · 3 copies · chains A, C, E, F

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

Pockets

13 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1162	0.76	0.78	105	empty
2	627	0.69	0.78	62	empty
3	500	0.68	0.79	50	empty
4	227	0.67	0.84	26	empty
5	266	0.63	0.81	22	empty

Interfaces

50 interfaces between chains.

C–H · 1867 Å² buried · 14 hydrogen bonds · protein-protein
E–F · 1787 Å² buried · 17 hydrogen bonds · protein-protein
A–B · 1781 Å² buried · 11 hydrogen bonds · protein-protein
D–G · 1723 Å² buried · 11 hydrogen bonds · protein-protein
K–L · 1669 Å² buried · 13 hydrogen bonds · protein-protein

Compared structures

6M2M · A role for histone chaperone OsChz1 in histone recognition and deposition · the same entry in another collection · chain O against O, 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 O81826
Every structure of UniProt Q9LQQ4
Every structure of UniProt Q2R2Z3
Elsewhere: RCSB PDB 6M2M · PDBe 6M2M · UniProt O81826 · UniProt Q9LQQ4 · UniProt Q2R2Z3

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