Research workbench

Drosophila HP1A chromo shadow domain

Analyse Drosophila HP1A chromo shadow domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3P7J
Type: protein
Length: 120 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Heterochromatin protein 1
UniProt: P05205

Structure

x-ray diffraction · 2 distinct chains · 35% helix, 37% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Heterochromatin protein 1	protein	59	29% helix, 37% strand	P05205
B	Heterochromatin protein 1	protein	61	41% helix, 36% strand	P05205

Ligands and binding sites

GOL · Glycerol · additive · chains B

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

Interfaces

1 interface between chains.

A–B · 547 Å² buried · 3 hydrogen bonds · protein-protein

Compared structures

3P7J · Drosophila HP1a chromo shadow domain · the same entry in another collection · chain A against A, TM-score 1.00
P05205 · AlphaFold monomer V2.0 prediction for heterochromatin protein 1 (P05205) · a predicted model of the same protein · chain A against A, TM-score 0.96

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 P05205
Elsewhere: RCSB PDB 3P7J · PDBe 3P7J · UniProt P05205

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.