Research workbench
Crystal structure of the catalytic core domain of human PHF8
Analyse Crystal structure of the catalytic core domain of human PHF8 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3K3N
- Type
- protein
- Length
- 349 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Phd finger protein 8
- EC
- 1.14.11.-
- UniProt
- Q5JPR9
- Ligands
- FE2
- Pockets
- 3 · best druggability 0.68
Structure
x-ray diffraction · 1 distinct chain · 39% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Phd finger protein 8 (EC 1.14.11.-) | protein | 349 | 39% helix, 23% strand | Q5JPR9 |
Ligands and binding sites
- FE2 · Fe (II) ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 509 | 0.68 | 0.78 | 54 | FE2 |
| 2 | 128 | 0.45 | 0.77 | 20 | empty |
| 3 | 79 | 0.35 | 0.76 | 19 | empty |
Compared structures
- 3K3N · Crystal structure of the catalytic core domain of human PHF8 · the same entry in another collection · chain A against A, 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 Q5JPR9
- Elsewhere: RCSB PDB 3K3N · PDBe 3K3N · UniProt Q5JPR9
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