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Structural basis of histone H4 recognition by P55

Analyse Structural basis of histone H4 recognition by P55 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3C99
Type: protein
Length: 380 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Chromatin assembly factor 1 P55 subunit
UniProt: Q24572
Ligands: CD
Pockets: 4 · best druggability 0.76

Structure

x-ray diffraction · 1 distinct chain · 9% helix, 43% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Chromatin assembly factor 1 P55 subunit	protein	380	9% helix, 43% strand	Q24572

Ligands and binding sites

CD · Cadmium ion · metal · 9 copies · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	442	0.76	0.84	31	empty
2	98	0.47	0.80	18	empty
3	100	0.33	0.72	16	empty
4	62	0.29	0.74	12	empty

Compared structures

3C99 · Structural Basis of Histone H4 Recognition by p55 · the same entry in another collection · chain A against A, TM-score 1.00
Q24572 · AlphaFold monomer V2.0 prediction for chromatin assembly factor 1 P55 subunit (Q24572) · a predicted model of the same protein · chain A against A, TM-score 0.98

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 Q24572
Elsewhere: RCSB PDB 3C99 · PDBe 3C99 · UniProt Q24572

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