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Crystal structure of sprlmcd

Analyse Crystal structure of sprlmcd in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5XJ1
Type
protein
Length
453 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Uncharacterized RNA methyltransferase SP_1029
EC
2.1.1.-
UniProt
Q97R12
Pockets
4 · best druggability 0.66

Structure

x-ray diffraction · 1 distinct chain · 26% helix, 33% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AUncharacterized RNA methyltransferase SP_1029 (EC 2.1.1.-)protein45326% helix, 33% strandQ97R12

Ligands and binding sites

  • GOL · Glycerol · additive · 2 copies · chains A
  • P6G · Hexaethylene glycol · additive · chains A
  • EPE · 4-(2-hydroxyethyl)-1-piperazine ethanesulfonic acid · additive · chains A

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
15680.660.7678P6G, EPE
21340.440.7619empty
3540.310.7611empty
4690.290.7318empty

Compared structures

  • 5XJ1 · Crystal structure of spRlmCD · the same entry in another collection · chain A against A, TM-score 1.00
  • Q97R12 · AlphaFold monomer V2.0 prediction for uncharacterized RNA methyltransferase SP_1029… · a predicted model of the same protein · chain A against A, TM-score 0.99

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