Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

5UQ6

PIG PURPLE ACID PHOSPHATASE COMPLEXED WITH PHOSPHATE IN TWO COORDINATION MODES ALONG WITH A BRIDGING HYDROXIDE ION

Summary for 5UQ6
Entry DOI10.2210/pdb5uq6/pdb
DescriptorTartrate-resistant acid phosphatase type 5, 2-acetamido-2-deoxy-beta-D-glucopyranose, FE (III) ION, ... (7 entities in total)
Functional Keywordstransition state, metallohydrolase, hydroxide., hydrolase
Biological sourceSus scrofa (Pig)
Total number of polymer chains1
Total formula weight35621.93
Authors
Selleck, C.,Guddat, L.,Schenk, G.,Clayton, D. (deposition date: 2017-02-06, release date: 2017-05-24, Last modification date: 2024-10-30)
Primary citationSelleck, C.,Clayton, D.,Gahan, L.R.,Mitic, N.,McGeary, R.P.,Pedroso, M.M.,Guddat, L.W.,Schenk, G.
Visualization of the Reaction Trajectory and Transition State in a Hydrolytic Reaction Catalyzed by a Metalloenzyme.
Chemistry, 23:4778-4781, 2017
Cited by
PubMed Abstract: Metallohydrolases are a vast family of enzymes that play crucial roles in numerous metabolic pathways. Several members have emerged as targets for chemotherapeutics. Knowledge about their reaction mechanisms and associated transition states greatly aids the design of potent and highly specific drug leads. By using a high-resolution crystal structure, we have probed the trajectory of the reaction catalyzed by purple acid phosphatase, an enzyme essential for the integrity of bone structure. In particular, the transition state is visualized, thus providing detailed structural information that may be exploited in the design of specific inhibitors for the development of new anti-osteoporotic chemotherapeutics.
PubMed: 28261912
DOI: 10.1002/chem.201700866
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.182 Å)
Structure validation

247947

PDB entries from 2026-01-21

PDB statisticsPDBj update infoContact PDBjnumon