Research workbench
Crystal structure of maf domain of human N-acetylserotonin O- methyltransferase-like protein soaked with tfbq
Analyse Crystal structure of maf domain of human N-acetylserotonin O… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6XI4
- 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
- CL, SO4
- Pockets
- 5 · best druggability 0.58
Structure
x-ray diffraction · 1 distinct chain · 40% 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 | 40% helix, 28% strand | O95671 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 190 | 0.58 | 0.80 | 26 | empty |
| 2 | 161 | 0.55 | 0.81 | 26 | SO4 |
| 3 | 222 | 0.51 | 0.75 | 22 | CL |
| 4 | 104 | 0.47 | 0.80 | 26 | SO4 |
| 5 | 86 | 0.35 | 0.74 | 13 | empty |
Interfaces
1 interface between chains.
- A–B · 920 Ų buried · 16 hydrogen bonds · protein-protein
Compared structures
- 6XI4 · Crystal structure of Maf domain of human N-acetylserotonin O-methyltransferase-like… · 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 0.99
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 O95671
- Elsewhere: RCSB PDB 6XI4 · PDBe 6XI4 · UniProt O95671
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