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Crystal structure of TAF14 yeats domain in complex with histone H3K9PR

Analyse Crystal structure of TAF14 yeats domain in complex with histone H3K9PR in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6MIO
Type: protein
Length: 148 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Transcription initiation factor tfiid subunit 14; Histone H3K9PR
UniProt: P35189
Ligands: ACE

Structure

x-ray diffraction · 2 distinct chains · 11% helix, 51% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Transcription initiation factor tfiid subunit 14	protein	142	12% helix, 52% strand	P35189
B	Histone H3K9PR	protein	6	0% helix, 17% strand	—

Ligands and binding sites

ACE · Acetyl group · ligand · chains A, B

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

Interfaces

1 interface between chains.

A–B · 502 Å² buried · 10 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 1 covalent, 1 modified (covalent ligand, nonstandard).

Compared structures

6MIO · Crystal structure of Taf14 YEATS domain in complex with histone H3K9pr · the same entry in another collection · chain A against A, TM-score 1.00
P35189 · AlphaFold monomer V2.0 prediction for transcription initiation factor tfiid subunit 14… · 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 P35189
Elsewhere: RCSB PDB 6MIO · PDBe 6MIO · UniProt P35189

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