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Solution structure of the TAF3 phd domain in complex with a H3K4ME3 peptide

Analyse Solution structure of the TAF3 phd domain in complex with a H3K4ME3 peptide in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2K17
Type: protein
Length: 88 residues
Chains: 2
Method: solution nmr
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: H3K4ME3 peptide; Transcription initiation factor tfiid subunit 3
UniProt: Q5HZG4
Ligands: ZN

Structure

solution nmr · 2 distinct chains · 10% helix, 22% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
P	H3K4ME3 peptide	protein	13	0% helix, 31% strand	—
A	Transcription initiation factor tfiid subunit 3	protein	75	12% helix, 20% strand	Q5HZG4

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.

P–A · 554 Å² buried · 13 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 1 modified (methylation).

Compared structures

2K17 · Solution structure of the TAF3 PHD domain in complex with a H3K4me3 peptide · the same entry in another collection · chain P against P, TM-score 1.00
Q5HZG4 · AlphaFold monomer V2.0 prediction for transcription initiation factor tfiid subunit 3… · a predicted model of the same protein · chain A against A, TM-score 0.81

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 Q5HZG4
Elsewhere: RCSB PDB 2K17 · PDBe 2K17 · UniProt Q5HZG4

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