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Crystal structure of a hairpin ribozyme in the catalytically-active conformation

Analyse Crystal structure of a hairpin ribozyme in the catalytically-active conformation in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1M5K
Type
protein + RNA
Length
410 residues
Chains
6
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
RNA inhibitor substrate; RNA hairpin ribozyme; Protein (U1 small nuclear…
UniProt
P09012
Ligands
CA, CL
Pockets
9 · best druggability 0.69

Structure

x-ray diffraction · 3 distinct chains · 33% helix, 26% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, DRNA inhibitor substraterna21——
B, ERNA hairpin ribozymerna92——
C, FProtein (U1 small nuclear ribonucleoprotein a)protein9233% helix, 26% strandP09012

Ligands and binding sites

  • CA · Calcium ion · metal · 33 copies · chains A, B, D, E, F
  • CL · Chloride ion · ion · 2 copies · chains F

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

Pockets

9 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
111900.690.7548CA
28160.670.7548CA, CL
36320.660.7631CA
47380.650.7541CA
54350.550.7424empty

Interfaces

5 interfaces between chains.

  • D–E · 1512 Ų buried · 94 hydrogen bonds · nucleic-nucleic
  • A–B · 1426 Ų buried · 101 hydrogen bonds · nucleic-nucleic
  • B–C · 931 Ų buried · 28 hydrogen bonds · protein-nucleic
  • E–F · 899 Ų buried · 33 hydrogen bonds · protein-nucleic
  • C–F · 224 Ų buried · 1 hydrogen bond · protein-protein

Modifications

Observed in the structure: 6 modified (nucleotide modification).

Compared structures

  • 1M5K · Crystal structure of a hairpin ribozyme in the catalytically-active conformation · the same entry in another collection · chain A against A, TM-score 1.00

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