Research workbench

Mutt pyrophosphohydrolase-metal-nucleotide-metal complex, NMR, 16 structures

Analyse Mutt pyrophosphohydrolase-metal-nucleotide-metal complex, NMR, 16 structures in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1TUM
Type: protein
Length: 129 residues
Chains: 1
Method: solution nmr
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Mutator mutt protein
EC: 3.6.1.-
UniProt: P08337
Ligands: APC, CON, MG
Pockets: 1 · best druggability 0.28

Structure

solution nmr · 1 distinct chain · 17% helix, 24% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Mutator mutt protein (EC 3.6.1.-)	protein	129	17% helix, 24% strand	P08337

Ligands and binding sites

APC · Diphosphomethylphosphonic acid adenosyl ester · ligand · chains A
CON · Cobalt tetraammine ion · ligand
MG · Magnesium ion · metal · 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	56	0.28	0.74	12	empty

Compared structures

1TUM · Mutt pyrophosphohydrolase-metal-nucleotide-metal complex, NMR, 16 structures · the same entry in another collection · chain A against A, TM-score 1.00
P08337 · AlphaFold monomer V2.0 prediction for 8-oxo-dgtp diphosphatase (P08337) · a predicted model of the same protein · chain A against A, TM-score 0.68

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 P08337
Elsewhere: RCSB PDB 1TUM · PDBe 1TUM · UniProt P08337

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