Research workbench
Crystal structure of FIBRILLARIN/NOP5P complex
Analyse Crystal structure of FIBRILLARIN/NOP5P complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1NT2
- Type
- protein
- Length
- 445 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Fibrillarin-like pre-rRNA processing protein; Conserved hypothetical protein
- UniProt
- O28192, O28191
- Ligands
- SAM
- Pockets
- 4 · best druggability 0.43
Structure
x-ray diffraction · 2 distinct chains · 50% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Fibrillarin-like pre-rRNA processing protein | protein | 209 | 31% helix, 31% strand | O28192 |
| B | Conserved hypothetical protein | protein | 236 | 67% helix, 3% strand | O28191 |
Ligands and binding sites
- SAM · S-adenosylmethionine · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 146 | 0.43 | 0.75 | 19 | empty |
| 2 | 118 | 0.42 | 0.77 | 27 | SAM |
| 3 | 96 | 0.41 | 0.77 | 20 | empty |
| 4 | 64 | 0.30 | 0.74 | 12 | empty |
Interfaces
1 interface between chains.
- A–B · 1374 Ų buried · 17 hydrogen bonds · protein-protein
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 O28192
- Every structure of UniProt O28191
- Elsewhere: RCSB PDB 1NT2 · PDBe 1NT2 · UniProt O28192 · UniProt O28191
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