Research workbench
Solution structure of human SAP18
Analyse Solution structure of human SAP18 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2HDE
- Type
- protein
- Length
- 148 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Histone deacetylase complex subunit SAP18
- UniProt
- O00422
Structure
solution nmr · 1 distinct chain · 15% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Histone deacetylase complex subunit SAP18 | protein | 148 | 15% helix, 24% strand | O00422 |
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 O00422
- Elsewhere: RCSB PDB 2HDE · PDBe 2HDE · UniProt O00422
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