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Crystal structure of bs-cspb in complex with R(GUCUUUA)

Analyse Crystal structure of bs-cspb in complex with R(GUCUUUA) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3PF4
Type: protein + RNA
Length: 137 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cold shock protein cspb; Hexaribonucleotide (rgucuuua)
UniProt: P32081
Ligands: NA, MG

Structure

x-ray diffraction · 2 distinct chains · 5% helix, 56% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Cold shock protein cspb	protein	66	5% helix, 56% strand	P32081
R	Hexaribonucleotide (rgucuuua)	rna	5	—	—

Ligands and binding sites

NA · Sodium ion · metal · chains A
MG · Magnesium ion · metal · chains A

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

Interfaces

3 interfaces between chains.

A–B · 541 Å² buried · 7 hydrogen bonds · protein-protein
B–R · 452 Å² buried · 6 hydrogen bonds · protein-nucleic
A–R · 41 Å² buried · 1 hydrogen bond · protein-nucleic

Compared structures

3PF4 · Crystal structure of Bs-CspB in complex with r(GUCUUUA) · the same entry in another collection · chain A against A, TM-score 1.00
P32081 · AlphaFold monomer V2.0 prediction for cold shock protein cspb (P32081) · a predicted model of the same protein · chain A against A, TM-score 0.94

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 P32081
Elsewhere: RCSB PDB 3PF4 · PDBe 3PF4 · UniProt P32081

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