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Crystal structure of TAF14 yeats domain in complex with histone H3K9CR

Analyse Crystal structure of TAF14 yeats domain in complex with histone H3K9CR in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5IOK
Type
protein
Length
149 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Transcription initiation factor tfiid subunit 14; (ACE)QTAR(KCR)ST
UniProt
P35189
Ligands
ACE

Structure

x-ray diffraction · 2 distinct chains · 9% helix, 50% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ATranscription initiation factor tfiid subunit 14protein14210% helix, 52% strandP35189
C(ACE)QTAR(KCR)STprotein70% helix, 14% strand—

Ligands and binding sites

  • ACE · Acetyl group · ligand · chains A, C
  • PEG · Di(hydroxyethyl)ether · additive · 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–C · 539 Ų buried · 10 hydrogen bonds · protein-protein

Modifications

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

Compared structures

  • 5IOK · Crystal structure of Taf14 YEATS domain in complex with histone H3K9cr · 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

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