MolNFT v1 · #122416 · protein
Crystal structure of TAF14 yeats domain in complex with histone H3K9CR
5IOK · Transcription initiation factor tfiid subunit 14: “Crystal structure of TAF14 yeats domain in complex with histone H3K9CR”. X-ray diffraction, 1 ligand (ACE). MolNFT v1 #122416 on GenesisL1: 3D structure, binding sites and pockets…
- 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).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Transcription initiation factor tfiid subunit 14 | protein | 142 | 10% helix, 52% strand | P35189 |
| C | (ACE)QTAR(KCR)ST | protein | 7 | 0% 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
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 5IOK · PDBe 5IOK · UniProt P35189
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