› 1mp2

X-ray diffraction
2.3Å resolution

Structure of MT-ADPRase (Apoenzyme), a Nudix hydrolase from Mycobacterium tuberculosis

Released:
DOI: 10.2210/pdb1mp2/pdb
Model geometry
Fit model/data
Data not deposited
PDB entry 1mp2 coloured by chain, front view.
PDB entry 1mp2 coloured by chain, side view.
PDB entry 1mp2 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

No bound ligands
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: RIGAKU RU200
Spacegroup: P6122
Unit cell:
a: 63.559Å b: 63.559Å c: 182.146Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.204 0.204 0.262
Expression system: Escherichia coli

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Citations

1 review citation

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

1 mention without citation

Identification of the ligand binding sites on the molecular surface of proteins.
Kinoshita et al. (2005)