MolNFT v1 · #31557 · protein

The structure of nucleosome assembly protein suggests a mechanism for histone binding and shuttling

2AYU: “The structure of nucleosome assembly protein suggests a mechanism for histone binding and shuttling”. X-ray diffraction, 5 pockets (best druggability 0.59). MolNFT v1 #31557 on GenesisL1: 3D structure, binding sites and pockets in…

PDB: 2AYU
Type: protein
Length: 283 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Nucleosome assembly protein
UniProt: P25293
Pockets: 5 · best druggability 0.59

Structure

x-ray diffraction · 1 distinct chain · 48% helix, 15% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Nucleosome assembly protein	protein	283	48% helix, 15% strand	P25293

Pockets

5 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	462	0.59	0.74	35	empty
2	50	0.45	0.84	13	empty
3	91	0.40	0.77	15	empty
4	69	0.35	0.77	19	empty
5	59	0.35	0.78	14	empty

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

2AYU · The structure of nucleosome assembly protein suggests a mechanism for histone binding and… · the same entry in another collection · chain A against A, TM-score 1.00
P25293 · AlphaFold monomer V2.0 prediction for nucleosome assembly protein (P25293) · a predicted model of the same protein · chain A against A, TM-score 0.97

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 P25293
Elsewhere: RCSB PDB 2AYU · PDBe 2AYU · UniProt P25293

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