Research workbench
Solution structure of the ASHH2 cw domain with the N-terminal histone H3 tail mimicking peptide monomethylated on lysine 4
Analyse Solution structure of the ASHH2 cw domain with the N-terminal histone H3 tail… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6QXZ
- Type
- protein
- Length
- 88 residues
- Chains
- 2
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Histone-lysine N-methyltransferase ASHH2; Ala-arg-thr-mlz-gln-thr-ala-arg-tyr
- EC
- 2.1.1.43
- UniProt
- Q2LAE1
- Ligands
- ZN
- Pockets
- 1 · best druggability 0.43
Structure
solution nmr · 2 distinct chains · 17% helix, 9% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Histone-lysine N-methyltransferase ASHH2 (EC 2.1.1.43) | protein | 79 | 19% helix, 10% strand | Q2LAE1 |
| B | Ala-arg-thr-mlz-gln-thr-ala-arg-tyr | protein | 9 | 0% helix, 0% strand | — |
Ligands and binding sites
- ZN · Zinc ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 86 | 0.43 | 0.79 | 15 | empty |
Interfaces
1 interface between chains.
- A–B · 818 Ų buried · 17 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 modified (methylation).
Compared structures
- 6QXZ · Solution structure of the ASHH2 CW domain with the N-terminal histone H3 tail mimicking… · the same entry in another collection · chain A against A, TM-score 1.00
- Q2LAE1 · AlphaFold monomer V2.0 prediction for histone-lysine N-methyltransferase ASHH2 (Q2LAE1) · a predicted model of the same protein · chain A against A, TM-score 0.68
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 Q2LAE1
- Elsewhere: RCSB PDB 6QXZ · PDBe 6QXZ · UniProt Q2LAE1
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