GL1X · GenesisL1 explorer

MolNFT v1 · #138879 · protein

Structure of taf phd finger domain binds to H3(1-15)K4AC

5WXG · Transcription initiation factor tfiid subunit 3: “Structure of taf phd finger domain binds to H3(1-15)K4AC”. X-ray diffraction, 2 ligands (ZN, MG). MolNFT v1 #138879 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB
5WXG
Type
protein
Length
70 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Transcription initiation factor tfiid subunit 3; Histone H3K4AC
UniProt
Q5VWG9
Ligands
ZN, MG

Structure

x-ray diffraction · 2 distinct chains · 6% helix, 24% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ATranscription initiation factor tfiid subunit 3protein636% helix, 22% strandQ5VWG9
PHistone H3K4ACprotein70% helix, 43% strand—

Ligands and binding sites

  • ZN · Zinc ion · metal · 2 copies · chains A
  • MG · Magnesium ion · metal · chains A, P

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

Interfaces

1 interface between chains.

  • A–P · 500 Ų buried · 15 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 1 modified (acetylation).

Compared structures

  • 5WXG · Structure of TAF PHD finger domain binds to H3(1-15)K4ac · the same entry in another collection · chain A against A, TM-score 1.00
  • Q5VWG9 · 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 0.89

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