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PDBe Entry: 1ptw view

The Crystal Structure of AMP-Bound PDE4 Suggests a Mechanism for Phosphodiesterase Catalysis
Summary
Header HYDROLASEsearch
Method X-RAY DIFFRACTION
Experiment Resolution: 2.3 Å, R-factor: 22.9%, Free R-factor: 27.4%, Spacegroup: P 21 21 21
Released 11/11/2003, deposition: 23/06/2003, last revision: 24/02/2009
Authors Huai, Q.search; Colicelli, J.search; Ke, H.search
Primary citation The crystal structure of AMP-bound PDE4 suggests a mechanism for phosphodiesterase catalysis
BIOCHEMISTRYsearch vol:42, pag:13220-13226 (2003) [PubMed ID 14609333 ]search
Keywords catalytic mechanismsearch, cAMP hydrolysis crystal structuresearch, binuclear catalysissearch, HYDROLASEsearch
EC 3.1.4.17 ExPASy BRENDA search (A B C D)
Organism Homo sapiens(human) 9606search(A B C D)
UniProt cAMP-specific 3',5'-cyclic phosphodiesterase 4D (EC 3.1.4.17) (DPDE3) (PDE43) Q08499search (A B C D)
Solvent A, B, C, D
Polymers
Id Name Type UniProt Residues Observed
A, B, C, D cAMP-specific phosphodiesterase PDE4D2 Protein Q08499 (PDE4D_HUMAN)search
360 92%
Heterogens
Id Name Ligands
A, B, C, D ZINC ION ZN search
A, B, C, D ADENOSINE MONOPHOSPHATE AMP search
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