Research workbench
Scm SAM domain
Analyse Scm SAM domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1PK3
- Type
- protein
- Length
- 222 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Sex comb on midleg CG9495-pa
- UniProt
- Q9VHA0
Structure
x-ray diffraction · 3 distinct chains · 71% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Sex comb on midleg CG9495-pa | protein | 76 | 72% helix, 0% strand | Q9VHA0 |
| B | Sex comb on midleg CG9495-pa | protein | 68 | 72% helix, 0% strand | Q9VHA0 |
| C | Sex comb on midleg CG9495-pa | protein | 78 | 69% helix, 0% strand | Q9VHA0 |
Ligands and binding sites
- BME · Beta-mercaptoethanol · additive · 3 copies · chains A, B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
2 interfaces between chains.
- B–C · 551 Ų buried · 5 hydrogen bonds · protein-protein
- A–B · 550 Ų buried · 4 hydrogen bonds · protein-protein
Compared structures
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 Q9VHA0
- Elsewhere: RCSB PDB 1PK3 · PDBe 1PK3 · UniProt Q9VHA0
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.