› 1mr2

X-ray diffraction
2.3Å resolution

Structure of the MT-ADPRase in complex with 1 Mn2+ ion and AMP-CP (a inhibitor), a nudix enzyme

Released:
DOI: 10.2210/pdb1mr2/pdb
PDB entry 1mr2 coloured by chain, front view.
PDB entry 1mr2 coloured by chain, side view.
PDB entry 1mr2 coloured by chain, top view.
Source organism: Mycobacterium tuberculosis
Primary publication:
Structure and mechanism of MT-ADPRase, a nudix hydrolase from Mycobacterium tuberculosis.
Kang LW, Gabelli SB, Cunningham JE, O'Handley SF, Amzel LM
Structure 11 1015-23 (2003)
PMID: 12906832

Function and Biology Details

Reaction catalysed: 
ADP-D-ribose + H(2)O = AMP + D-ribose 5-phosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-128473 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Nudix hydrolase domain-containing protein Chain: A
Molecule details ›
Chain: A
Length: 207 amino acids
Theoretical weight: 22.92 KDa
Source organism: Mycobacterium tuberculosis
Expression system: Escherichia coli
UniProt:
  • Canonical: O33199 (Residues: 1-207; Coverage: 100%)
Gene name: MT1739
Sequence domains: NUDIX domain
Structure domains: Nucleoside Triphosphate Pyrophosphohydrolase

Ligands and Environments

2 bound ligands:
Ligand MN 1 x MN
Ligand A12 1 x A12
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P6122
Unit cell:
a: 63.894Å b: 63.894Å c: 182.059Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.205 0.205 0.26
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Structures and mechanisms of Nudix hydrolases.
Mildvan et al. (2005)
41 other articles

1 mention without citation

Discovery of holoenzyme-disrupting chemicals as substrate-selective CK2 inhibitors.
Kufareva et al. (2019)