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Molecular basis of histone H3K36ME3 recognition by the pwwp domain of BRPF1.

Analyse Molecular basis of histone H3K36ME3 recognition by the pwwp domain of BRPF1. in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2X35
Type: protein
Length: 125 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Peregrin
UniProt: P55201
Pockets: 2 · best druggability 0.29

Structure

x-ray diffraction · 1 distinct chain · 34% helix, 24% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Peregrin	protein	125	34% helix, 24% strand	P55201

Pockets

2 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	54	0.29	0.75	13	empty
2	52	0.27	0.74	18	empty

Compared structures

2X35 · Molecular basis of Histone H3K36me3 recognition by the PWWP domain of BRPF1. · the same entry in another collection · chain A against A, TM-score 1.00
P55201 · AlphaFold monomer V2.0 prediction for peregrin (P55201) · 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 P55201
Elsewhere: RCSB PDB 2X35 · PDBe 2X35 · UniProt P55201

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