Research workbench
Complex structure of PHF19
Analyse Complex structure of PHF19 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6WAU
- Type
- protein
- Length
- 385 residues
- Chains
- 12
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Phd finger protein 19; Histone H3.1T peptide
- UniProt
- Q5T6S3, Q16695
- Ligands
- UNX
- Pockets
- 2 · best druggability 0.66
Structure
x-ray diffraction · 8 distinct chains · 5% helix, 48% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Phd finger protein 19 | protein | 57 | 5% helix, 49% strand | Q5T6S3 |
| B | Phd finger protein 19 | protein | 56 | 5% helix, 50% strand | Q5T6S3 |
| C | Phd finger protein 19 | protein | 56 | 5% helix, 50% strand | Q5T6S3 |
| D, F | Phd finger protein 19 | protein | 55 | 5% helix, 51% strand | Q5T6S3 |
| E | Phd finger protein 19 | protein | 52 | 6% helix, 56% strand | Q5T6S3 |
| G, H, J, K | Histone H3.1T peptide | protein | 9 | 0% helix, 11% strand | Q16695 |
| I | Histone H3.1T peptide | protein | 10 | 0% helix, 10% strand | Q16695 |
| L | Histone H3.1T peptide | protein | 8 | 0% helix, 13% strand | Q16695 |
Ligands and binding sites
- UNX · Unknown atom or ion · ion · 11 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 475 | 0.66 | 0.78 | 43 | empty |
| 2 | 419 | 0.60 | 0.76 | 40 | empty |
Interfaces
20 interfaces between chains.
- A–G · 473 Ų buried · 6 hydrogen bonds · protein-protein
- F–L · 472 Ų buried · 7 hydrogen bonds · protein-protein
- B–H · 466 Ų buried · 7 hydrogen bonds · protein-protein
- D–J · 464 Ų buried · 6 hydrogen bonds · protein-protein
- C–I · 456 Ų buried · 5 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 6 modified (methylation).
Compared structures
- 6WAU · Complex structure of PHF19 · the same entry in another collection · chain L against L, TM-score 1.00
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 Q5T6S3
- Every structure of UniProt Q16695
- Elsewhere: RCSB PDB 6WAU · PDBe 6WAU · UniProt Q5T6S3 · UniProt Q16695
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