MolNFT v1 · #135666 · protein

Crystal structure of eed in complex with H3K27ME3 peptide and 3- (BENZO[D][1,3]DIOXOL-4-YLMETHYL)PIPERIDINE-1-carboximidamide

5U5T: “Crystal structure of eed in complex with H3K27ME3 peptide and 3…”. X-ray diffraction, 2 ligands (7W7, YT3). MolNFT v1 #135666 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 5U5T
Type: protein
Length: 750 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt: O75530, Q15910
Ligands: 7W7, YT3

Structure

x-ray diffraction · 4 distinct chains.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	—	protein	348	—	O75530
B	—	protein	348	—	O75530
C	—	protein	26	—	Q15910
D	—	protein	28	—	Q15910

Ligands and binding sites

7W7 · (3R)-3-[(2H-1,3-benzodioxol-4-yl)methyl]piperidine-1-carboximidamide · ligand · 2 copies · chains A, B
YT3 · Yttrium (III) ion · metal · 2 copies · chains B

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

Compared structures

5U5T · Crystal structure of EED in complex with H3K27Me3 peptide and… · the same entry in another collection · chain D against D, TM-score 1.00
O75530 · AlphaFold monomer V2.0 prediction for polycomb protein eed (O75530) · a predicted model of the same protein · chain B against A, TM-score 1.00
Q15910 · AlphaFold monomer V2.0 prediction for histone-lysine N-methyltransferase EZH2 (Q15910) · a predicted model of the same protein · chain C against A, TM-score 0.90

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 O75530
Every structure of UniProt Q15910
Elsewhere: RCSB PDB 5U5T · PDBe 5U5T · UniProt O75530 · UniProt Q15910

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