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Crystal structure of PHORPP38 bound to a K-turn in P12.1 helix

Analyse Crystal structure of PHORPP38 bound to a K-turn in P12.1 helix in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5Y7M
Type
protein + RNA
Length
352 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
50S ribosomal protein L7AE; RNA (52-mer)
UniProt
P62009
Ligands
GTP, SO4
Pockets
4 · best druggability 0.36

Structure

x-ray diffraction · 2 distinct chains · 51% helix, 15% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, C50S ribosomal protein L7AEprotein12551% helix, 15% strandP62009
B, DRNA (52-mer)rna51——

Ligands and binding sites

  • GTP · Guanosine-5'-triphosphate · ligand · 2 copies · chains B, D
  • SO4 · Sulfate ion · ion · 9 copies · chains A, B, C, D

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

Pockets

4 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11120.360.7421empty
2920.340.7517empty
3940.310.7317SO4
4850.300.7413SO4

Interfaces

4 interfaces between chains.

  • A–B · 647 Ų buried · 25 hydrogen bonds · protein-nucleic
  • C–D · 640 Ų buried · 21 hydrogen bonds · protein-nucleic
  • A–D · 604 Ų buried · 15 hydrogen bonds · protein-nucleic
  • B–C · 597 Ų buried · 15 hydrogen bonds · protein-nucleic

Modifications

Observed in the structure: 2 covalent (covalent ligand).

Compared structures

  • 5Y7M · Crystal structure of PhoRpp38 bound to a K-turn in P12.1 helix · the same entry in another collection · chain A against A, TM-score 1.00
  • P62009 · AlphaFold monomer V2.0 prediction for 50S ribosomal protein L7AE (P62009) · a predicted model of the same protein · chain C against A, TM-score 0.96

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