Research workbench
Crystal structure of NSD3 tandem PHD5-C5HCH domains
Analyse Crystal structure of NSD3 tandem PHD5-C5HCH domains in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4GND
- Type
- protein
- Length
- 205 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Histone-lysine N-methyltransferase NSD3
- EC
- 2.1.1.43
- UniProt
- Q9BZ95
- Ligands
- ZN
Structure
x-ray diffraction · 2 distinct chains · 8% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Histone-lysine N-methyltransferase NSD3 (EC 2.1.1.43) | protein | 98 | 9% helix, 14% strand | Q9BZ95 |
| C | Histone-lysine N-methyltransferase NSD3 (EC 2.1.1.43) | protein | 107 | 7% helix, 16% strand | Q9BZ95 |
Ligands and binding sites
- ZN · Zinc ion · metal · 8 copies · chains A, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- A–C · 68 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 4GND · Crystal Structure of NSD3 tandem PHD5-C5HCH domains · the same entry in another collection · chain A against A, TM-score 1.00
- Q9BZ95 · AlphaFold monomer V2.0 prediction for histone-lysine N-methyltransferase NSD3 (Q9BZ95) · a predicted model of the same protein · chain A against A, TM-score 0.95
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 Q9BZ95
- Elsewhere: RCSB PDB 4GND · PDBe 4GND · UniProt Q9BZ95
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