Research workbench
Human SRP19 in complex with helix 6 of human srp RNA
Analyse Human SRP19 in complex with helix 6 of human srp RNA in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1JID
- Type
- protein + RNA
- Length
- 143 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Helix 6 of human srp RNA; Signal recognition particle 19 kda protein
- UniProt
- P09132
- Ligands
- MG
- Pockets
- 2 · best druggability 0.70
Structure
x-ray diffraction · 2 distinct chains · 30% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| B | Helix 6 of human srp RNA | rna | 29 | — | — |
| A | Signal recognition particle 19 kda protein | protein | 114 | 30% helix, 13% strand | P09132 |
Ligands and binding sites
- MG · Magnesium ion · metal · 2 copies · chains B
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 | 680 | 0.70 | 0.78 | 51 | MG |
| 2 | 74 | 0.43 | 0.80 | 18 | empty |
Interfaces
1 interface between chains.
- B–A · 729 Ų buried · 19 hydrogen bonds · protein-nucleic
Modifications
Observed in the structure: 3 modified (nucleotide modification).
Compared structures
- 1JID · Human SRP19 in complex with helix 6 of Human SRP RNA · the same entry in another collection · chain B against B, TM-score 1.00
- P09132 · AlphaFold monomer V2.0 prediction for signal recognition particle 19 kda protein (P09132) · a predicted model of the same protein · chain A against A, TM-score 0.97
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 P09132
- Elsewhere: RCSB PDB 1JID · PDBe 1JID · UniProt P09132
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