Research workbench

Human M7GPPPN-mRNA hydrolase (DCP2, NUDT20) catalytic domain

Analyse Human M7GPPPN-mRNA hydrolase (DCP2, NUDT20) catalytic domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5MP0
Type: protein
Length: 149 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: M7GPPPN-mRNA hydrolase
EC: 3.6.1.62
UniProt: Q8IU60
Pockets: 1 · best druggability 0.51

Structure

x-ray diffraction · 1 distinct chain · 25% helix, 27% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
D	M7GPPPN-mRNA hydrolase (EC 3.6.1.62)	protein	149	25% helix, 27% strand	Q8IU60

Ligands and binding sites

EDO · 1,2-ethanediol · additive · 2 copies · chains D

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	164	0.51	0.78	32	empty

Compared structures

5MP0 · Human m7GpppN-mRNA Hydrolase (DCP2, NUDT20) Catalytic Domain · the same entry in another collection · chain D against D, TM-score 1.00
Q8IU60 · AlphaFold monomer V2.0 prediction for M7GPPPN-mRNA hydrolase (Q8IU60) · a predicted model of the same protein · chain D against A, TM-score 0.89

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt Q8IU60
Elsewhere: RCSB PDB 5MP0 · PDBe 5MP0 · UniProt Q8IU60

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