Research workbench
Structural basis for specific substrate recognition by the chloroplast signal recognition particle protein CPSRP43
Analyse Structural basis for specific substrate recognition by the chloroplast signal… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3DEO
- Type
- protein
- Length
- 183 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Signal recognition particle 43 kda protein
- UniProt
- O22265
- Ligands
- MG
Structure
x-ray diffraction · 1 distinct chain · 48% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Signal recognition particle 43 kda protein | protein | 183 | 48% helix, 12% strand | O22265 |
Ligands and binding sites
- MG · Magnesium ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 3DEO · Structural basis for specific substrate recognition by the chloroplast signal recognition… · the same entry in another collection · chain A against A, TM-score 1.00
- O22265 · AlphaFold monomer V2.0 prediction for signal recognition particle 43 kda protein… · 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 O22265
- Elsewhere: RCSB PDB 3DEO · PDBe 3DEO · UniProt O22265
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