1MR2

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

Summary for 1MR2

• Entry DOI: 10.2210/pdb1mr2/pdb
• Related: 1mk1 1mp2 1MQE 1MQW
• Descriptor: ADPR pyrophosphatase, MANGANESE (II) ION, PHOSPHOMETHYLPHOSPHONIC ACID ADENOSYL ESTER, ... (4 entities in total)
• Functional Keywords: nudix hydrolase, rv1700, adpr, mycobacterium tuberculosis, hydrolase
• Biological source: Mycobacterium tuberculosis
• Total number of polymer chains: 1
• Total formula weight: 23401.01

Authors

Kang, L.-W.,Gabelli, S.B.,Bianchet, M.A.,Cunningham, J.E.,O'Handley, S.F.,Amzel, L.M. (deposition date: 2002-09-17, release date: 2003-08-05, Last modification date: 2024-02-14)

Primary citation

Kang, L.-W.,Gabelli, S.B.,Cunningham, J.E.,O'Handley, S.F.,Amzel, L.M.
Structure and mechanism of MT-ADPRase, a Nudix hydrolase from Mycobacterium tuberculosis
Structure, 11:1015-1023, 2003

PubMed Abstract: Nudix hydrolases are a family of proteins that contain the characteristic sequence GX(5)EX(7)REUXEEXG(I/L/V), the Nudix box. They catalyze the hydrolysis of a variety of nucleoside diphosphate derivatives such as ADP-ribose, Ap(n)A (3 PubMed: 12906832
DOI: 10.1016/S0969-2126(03)00154-0

Experimental method

X-RAY DIFFRACTION (2.3 Å)