Research workbench
Sant domain of human DNA methyltransferase 1 associated protein 1
Analyse Sant domain of human DNA methyltransferase 1 associated protein 1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3HM5
- Type
- protein
- Length
- 74 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- DNA methyltransferase 1-associated protein 1
- UniProt
- Q9NPF5
- Ligands
- CA, UNX
Structure
x-ray diffraction · 1 distinct chain · 62% helix, 3% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | DNA methyltransferase 1-associated protein 1 | protein | 74 | 62% helix, 3% strand | Q9NPF5 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 3HM5 · SANT domain of human DNA methyltransferase 1 associated protein 1 · the same entry in another collection · chain A against A, TM-score 1.00
- Q9NPF5 · AlphaFold monomer V2.0 prediction for DNA methyltransferase 1-associated protein 1… · a predicted model of the same protein · chain A against A, TM-score 0.99
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 Q9NPF5
- Elsewhere: RCSB PDB 3HM5 · PDBe 3HM5 · UniProt Q9NPF5
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