Research workbench
Structure of human USB1 with adenosine 5'-monophosphate
Analyse Structure of human USB1 with adenosine 5'-monophosphate in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6D31
- Type
- protein
- Length
- 188 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- U6 snrna phosphodiesterase
- EC
- 3.1.4.-
- UniProt
- Q9BQ65
- Ligands
- AMP, CL
- Pockets
- 1 · best druggability 0.50
Structure
x-ray diffraction · 1 distinct chain · 36% helix, 31% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | U6 snrna phosphodiesterase (EC 3.1.4.-) | protein | 188 | 36% helix, 31% strand | Q9BQ65 |
Ligands and binding sites
- AMP · Adenosine monophosphate · ligand · chains A
- CL · Chloride ion · ion · chains A
- GOL · Glycerol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 227 | 0.50 | 0.75 | 32 | AMP |
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 Q9BQ65
- Elsewhere: RCSB PDB 6D31 · PDBe 6D31 · UniProt Q9BQ65
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