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Crystal structure of nudix hydrolase DR1025 in complex with SM+3

Analyse Crystal structure of nudix hydrolase DR1025 in complex with SM+3 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1SOI
Type: protein
Length: 156 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: MUTT/NUDIX family protein
UniProt: Q9RVK2
Ligands: SM
Pockets: 1 · best druggability 0.31

Structure

x-ray diffraction · 1 distinct chain · 22% helix, 33% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	MUTT/NUDIX family protein	protein	156	22% helix, 33% strand	Q9RVK2

Ligands and binding sites

SM · Samarium (III) ion · metal · 3 copies · chains A

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

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	79	0.31	0.73	20	empty

Compared structures

1SOI · Crystal structure of nudix hydrolase DR1025 in complex with SM+3 · the same entry in another collection · chain A against A, TM-score 1.00

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 Q9RVK2
Elsewhere: RCSB PDB 1SOI · PDBe 1SOI · UniProt Q9RVK2

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