Research workbench
Crystal structure of human N-acetylserotonin O-methyltransferase-like protein soaked with pdhptao
Analyse Crystal structure of human N-acetylserotonin O-methyltransferase-like protein… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6XI5
- Type
- protein
- Length
- 408 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Probable bifunctional DTTP/UTP PYROPHOSPHATASE/METHYLTRANSFERASE protein
- EC
- 3.6.1.9, 2.1.1.-
- UniProt
- O95671
- Ligands
- SO4
- Pockets
- 4 · best druggability 0.64
Structure
x-ray diffraction · 1 distinct chain · 39% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Probable bifunctional DTTP/UTP PYROPHOSPHATASE/METHYLTRANSFERASE protein (EC 3.6.1.9, 2.1.1.-) | protein | 204 | 39% helix, 28% strand | O95671 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 356 | 0.64 | 0.79 | 48 | empty |
| 2 | 219 | 0.53 | 0.76 | 25 | empty |
| 3 | 76 | 0.46 | 0.82 | 23 | empty |
| 4 | 56 | 0.29 | 0.74 | 11 | empty |
Interfaces
1 interface between chains.
- A–B · 1021 Ų buried · 13 hydrogen bonds · protein-protein
Compared structures
- 6XI5 · Crystal structure of human N-acetylserotonin O-methyltransferase-like protein soaked with… · the same entry in another collection · chain A against A, TM-score 1.00
- O95671 · AlphaFold monomer V2.0 prediction for probable bifunctional DTTP/UTP… · a predicted model of the same protein · chain A against A, TM-score 0.98
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 O95671
- Elsewhere: RCSB PDB 6XI5 · PDBe 6XI5 · UniProt O95671
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