Research workbench
The three-dimensional structure and X-ray sequence reveal that trichomaglin is a novel S-like ribonuclease
Analyse The three-dimensional structure and X-ray sequence reveal that trichomaglin is… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1SGL
- Type
- protein
- Length
- 206 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Trichomaglin
- EC
- 3.1.-.-
- UniProt
- P84146
- Ligands
- SO4
- Pockets
- 2 · best druggability 0.52
Structure
x-ray diffraction · 1 distinct chain · 33% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Trichomaglin (EC 3.1.-.-) | protein | 206 | 33% helix, 21% strand | P84146 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 4 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 133 | 0.52 | 0.81 | 25 | empty |
| 2 | 55 | 0.38 | 0.80 | 14 | empty |
Modifications
Observed in the structure: 7 disulfide (disulfide).
Compared structures
- 1SGL · The three-dimensional structure and X-ray sequence reveal that trichomaglin is a novel… · the same entry in another collection · chain A against A, TM-score 1.00
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 P84146
- Elsewhere: RCSB PDB 1SGL · PDBe 1SGL · UniProt P84146
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