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Crystal structure of the deah-box ATPase PRP2 in complex with SPP2 and ADP

Analyse Crystal structure of the deah-box ATPase PRP2 in complex with SPP2 and ADP in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6RM9
Type
protein
Length
695 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Putative mRNA splicing factor; Putative pre-mRNA splicing protein
UniProt
G0SEG4, G0SFN3
Ligands
ADP, MG
Pockets
9 · best druggability 0.80

Structure

x-ray diffraction · 2 distinct chains · 44% helix, 18% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
APutative mRNA splicing factorprotein65545% helix, 19% strandG0SEG4
CPutative pre-mRNA splicing proteinprotein4028% helix, 0% strandG0SFN3

Ligands and binding sites

  • ADP · Adenosine-5'-diphosphate · ligand · chains A
  • MG · Magnesium ion · metal · chains A
  • ACT · Acetate ion · additive · 2 copies · chains A
  • GOL · Glycerol · additive · 2 copies · chains A
  • PEG · Di(hydroxyethyl)ether · additive · chains A, C

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
15480.800.8676ACT, GOL
24080.740.8464ADP, MG, ACT
32040.690.8738empty
41040.670.9121empty
5930.590.8723empty

Interfaces

1 interface between chains.

  • A–C · 1588 Ų buried · 12 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 1 modified (oxidation).

Compared structures

  • 6RM9 · Crystal structure of the DEAH-box ATPase Prp2 in complex with Spp2 and ADP · the same entry in another collection · chain A against A, TM-score 1.00

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