Structure of PDB 3rl3 Chain A

Receptor sequence
>3rl3A (length=276) Species: 10116 (Rattus norvegicus) [Search protein sequence]
VTITVDEYSSNPTQAFTHYNINQSRFQPPHVHMVDPIPYDTPKPAGHTRF
VCISDTHSRTDGIQMPYGDILLHTGDFTELGLPSEVKKFNDWLGNLPYEY
KIVIAGNHELTFDKEFMADLVRFPSVSKLKPEDFDNVQSLLTNSIYLQDS
EVTVKGFRIYGAPWTPWFNGWGFNLPRGQSLLDKWNLIPEGTDILMTHGP
PLGFRDWVPKELQRVGCVELLNTVQRRVRPKLHVFGGIHEGYGTMTDGYT
TYINASTCTVSFQPTNPPIIFDLPNP
3D structure
PDB3rl3 Unique utilization of a phosphoprotein phosphatase fold by a mammalian phosphodiesterase associated with WAGR syndrome.
ChainA
Resolution1.42 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 3.1.-.-
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 MN A D65 H67 D86 H254 D55 H57 D76 H239
BS02 MN A D86 N117 H213 D76 N107 H198
BS03 MN A E147 D150 N151 E132 D135 N136
BS04 MN A E205 G206 V243 E190 G191 V228
BS05 MN A G206 D208 G191 D193
BS06 5GP A H67 D86 N117 H118 F183 K225 I253 H254 E255 H57 D76 N107 H108 F168 K210 I238 H239 E240 MOAD: ic50=67nM
PDBbind-CN: -logKd/Ki=7.17,IC50=67nM
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0008081 phosphoric diester hydrolase activity
GO:0016208 AMP binding
GO:0016787 hydrolase activity
GO:0019002 GMP binding
GO:0030145 manganese ion binding
GO:0046872 metal ion binding

View graph for
Molecular Function
External links
PDB RCSB:3rl3, PDBe:3rl3, PDBj:3rl3
PDBsum3rl3
PubMed21824479
UniProtB1WBP0|MPPD2_RAT Metallophosphoesterase MPPED2 (Gene Name=Mpped2)

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