Research workbench
Crystal structure of C. crescentus pnpase bound to RNase E recognition peptide
Analyse Crystal structure of C. crescentus pnpase bound to RNase E recognition peptide in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4AID
- Type
- protein
- Length
- 1,690 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q9AC32, Q9A749
Structure
x-ray diffraction · 6 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 573 | — | Q9AC32 |
| B | — | protein | 558 | — | Q9AC32 |
| C | — | protein | 539 | — | Q9AC32 |
| F | — | protein | 7 | — | Q9A749 |
| G | — | protein | 8 | — | Q9A749 |
| H | — | protein | 5 | — | Q9A749 |
Compared structures
- 4AID · Crystal structure of C. crescentus PNPase bound to RNase E recognition peptide · the same entry in another collection · chain H against H, TM-score 1.00
- Q9AC32 · AlphaFold monomer V2.0 prediction for polyribonucleotide nucleotidyltransferase (Q9AC32) · a predicted model of the same protein · chain C against A, TM-score 0.96
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 Q9AC32
- Every structure of UniProt Q9A749
- Elsewhere: RCSB PDB 4AID · PDBe 4AID · UniProt Q9AC32 · UniProt Q9A749
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