MolNFT v1 · #140164 · protein

Crystal structure of AL1 phd finger bound to H3K4ME3

5Y20 · Phd finger protein alfin-like 1: “Crystal structure of AL1 phd finger bound to H3K4ME3”. X-ray diffraction, 1 ligand (ZN). MolNFT v1 #140164 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 5Y20
Type: protein
Length: 59 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Phd finger protein alfin-like 1; Peptide from histone H3
UniProt: Q9FFF5
Ligands: ZN

Structure

x-ray diffraction · 2 distinct chains · 15% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Phd finger protein alfin-like 1	protein	52	17% helix, 15% strand	Q9FFF5
P	Peptide from histone H3	protein	7	0% helix, 29% strand	—

Ligands and binding sites

ZN · Zinc ion · metal · 2 copies · chains A

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

Interfaces

1 interface between chains.

A–P · 561 Å² buried · 9 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 1 modified (methylation).

Compared structures

5Y20 · Crystal structure of AL1 PHD finger bound to H3K4me3 · the same entry in another collection · chain A against A, TM-score 1.00
Q9FFF5 · AlphaFold monomer V2.0 prediction for phd finger protein alfin-like 1 (Q9FFF5) · a predicted model of the same protein · chain A against A, TM-score 0.95

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 Q9FFF5
Elsewhere: RCSB PDB 5Y20 · PDBe 5Y20 · UniProt Q9FFF5

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