MolNFT v1 · #35049 · protein

Crystal structure of histone chaperone ASF1 in complex with a C-terminus of histone H3

2DZE · Histone chaperone CIA1: “Crystal structure of histone chaperone ASF1 in complex with a C-terminus of histone H3”. X-ray diffraction, 3 pockets (best druggability 0.41). MolNFT v1 #35049 on GenesisL1: 3D structure, binding sites and…

PDB: 2DZE
Type: protein
Length: 326 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Histone chaperone CIA1; 10-mer peptide from histone H3.1/H3.2
UniProt: O74515, P09988
Pockets: 3 · best druggability 0.41

Structure

x-ray diffraction · 3 distinct chains · 10% helix, 49% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Histone chaperone CIA1	protein	160	10% helix, 48% strand	O74515
B	Histone chaperone CIA1	protein	160	10% helix, 49% strand	O74515
X	10-mer peptide from histone H3.1/H3.2	protein	6	0% helix, 67% strand	P09988

Ligands and binding sites

PGE · Triethylene glycol · additive · 2 copies · chains A, B

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

Pockets

3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	106	0.41	0.76	22	empty
2	69	0.32	0.74	16	empty
3	58	0.31	0.75	18	empty

Interfaces

3 interfaces between chains.

B–X · 446 Å² buried · 6 hydrogen bonds · protein-protein
A–X · 365 Å² buried · 10 hydrogen bonds · protein-protein
A–B · 13 Å² buried · 0 hydrogen bonds · protein-protein

Compared structures

2DZE · Crystal structure of histone chaperone Asf1 in complex with a C-terminus of histone H3 · the same entry in another collection · chain A against A, TM-score 1.00
O74515 · AlphaFold monomer V2.0 prediction for histone chaperone CIA1 (O74515) · a predicted model of the same protein · chain B against A, TM-score 0.98
P09988 · AlphaFold monomer V2.0 prediction for histone H3.1/H3.2 (P09988) · a predicted model of the same protein · chain X against A, TM-score 0.69

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 O74515
Every structure of UniProt P09988
Elsewhere: RCSB PDB 2DZE · PDBe 2DZE · UniProt O74515 · UniProt P09988

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