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Crystal structure of a putative RNA methyltransferase PH1948 from pyrococcus horikoshii

Analyse Crystal structure of a putative RNA methyltransferase PH1948 from pyrococcus… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1WY7
Type
protein
Length
799 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Hypothetical protein PH1948
EC
2.1.1.-
UniProt
O59611
Ligands
SAH
Pockets
17 · best druggability 0.69

Structure

x-ray diffraction · 4 distinct chains · 36% helix, 26% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AHypothetical protein PH1948 (EC 2.1.1.-)protein19636% helix, 27% strandO59611
BHypothetical protein PH1948 (EC 2.1.1.-)protein19837% helix, 27% strandO59611
CHypothetical protein PH1948 (EC 2.1.1.-)protein20136% helix, 26% strandO59611
DHypothetical protein PH1948 (EC 2.1.1.-)protein20436% helix, 25% strandO59611

Ligands and binding sites

  • SAH · S-adenosyl-L-homocysteine · ligand · 4 copies · chains A, B, C, D

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11500.690.8930SAH
21830.670.8633SAH
31550.670.8733SAH
41550.660.8731SAH
52600.600.7925empty

Interfaces

3 interfaces between chains.

  • B–D · 486 Ų buried · 13 hydrogen bonds · protein-protein
  • A–C · 412 Ų buried · 12 hydrogen bonds · protein-protein
  • A–B · 274 Ų buried · 0 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 9 modified (engineered).

Compared structures

  • 1WY7 · crystal structure of a putative RNA methyltransferase PH1948 from Pyrococcus horikoshii · the same entry in another collection · chain A against A, TM-score 1.00

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