MolNFT v1 · #134662 · protein
Solution NMR structure of PHF20 phd domain in complex with a histone H3K4ME2 peptide
5TBN · Phd finger protein 20: “Solution NMR structure of PHF20 phd domain in complex with a histone H3K4ME2 peptide”. Solution nmr, 2 ligands (ZN, NH2). MolNFT v1 #134662 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 5TBN
- Type
- protein
- Length
- 68 residues
- Chains
- 2
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Phd finger protein 20; Histone H3.1
- UniProt
- Q9BVI0, P68431
- Ligands
- ZN, NH2
Structure
solution nmr · 2 distinct chains · 6% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Phd finger protein 20 | protein | 57 | 7% helix, 16% strand | Q9BVI0 |
| C | Histone H3.1 | protein | 11 | 0% helix, 27% strand | P68431 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- A–C · 472 Ų buried · 8 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 modified (methylation).
Compared structures
- 5TBN · Solution NMR structure of PHF20 PHD domain in complex with a histone H3K4me2 peptide · the same entry in another collection · chain A against A, TM-score 1.00
- Q9BVI0 · AlphaFold monomer V2.0 prediction for phd finger protein 20 (Q9BVI0) · a predicted model of the same protein · chain A against A, TM-score 0.74
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 Q9BVI0
- Every structure of UniProt P68431
- Elsewhere: RCSB PDB 5TBN · PDBe 5TBN · UniProt Q9BVI0 · UniProt P68431
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