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Crystal structure of rlmh in complex with S-adenosylmethionine

Analyse Crystal structure of rlmh in complex with S-adenosylmethionine in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5TWJ
Type
protein
Length
628 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Ribosomal RNA large subunit methyltransferase H
EC
2.1.1.177
UniProt
B7MFQ9
Ligands
SAM
Pockets
7 · best druggability 0.80

Structure

x-ray diffraction · 1 distinct chain · 45% helix, 20% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
C, D, A, BRibosomal RNA large subunit methyltransferase H (EC 2.1.1.177)protein15745% helix, 20% strandB7MFQ9

Ligands and binding sites

  • SAM · S-adenosylmethionine · ligand · 4 copies · chains C, D, A, B

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
18660.800.8365SAM
24040.640.7847SAM
33820.620.7742SAM
41610.580.8225SAM
51420.430.7519empty

Interfaces

4 interfaces between chains.

  • A–B · 1137 Ų buried · 7 hydrogen bonds · protein-protein
  • C–D · 1098 Ų buried · 6 hydrogen bonds · protein-protein
  • D–A · 435 Ų buried · 15 hydrogen bonds · protein-protein
  • C–A · 334 Ų buried · 7 hydrogen bonds · protein-protein

Compared structures

  • 5TWJ · Crystal Structure of RlmH in Complex with S-Adenosylmethionine · the same entry in another collection · chain B against B, TM-score 1.00
  • B7MFQ9 · AlphaFold monomer V2.0 prediction for ribosomal RNA large subunit methyltransferase H… · a predicted model of the same protein · chain A against A, TM-score 0.98

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