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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: 3DEP
Type: protein
Length: 195 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Signal recognition particle 43 kda protein; Ypggsfdplgla
UniProt: O22265
Ligands: CL

Structure

x-ray diffraction · 2 distinct chains · 45% helix, 13% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Signal recognition particle 43 kda protein	protein	183	48% helix, 14% strand	O22265
B	Ypggsfdplgla	protein	12	0% helix, 0% strand	—

Ligands and binding sites

CL · Chloride ion · ion · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Interfaces

1 interface between chains.

A–B · 518 Å² buried · 7 hydrogen bonds · protein-protein

Compared structures

3DEP · Structural basis for specific substrate recognition by the chloroplast signal recognition… · the same entry in another collection · chain B against B, 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

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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 3DEP · PDBe 3DEP · UniProt O22265

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