Structure of PDB 1jp4 Chain A

Receptor sequence
>1jp4A (length=302) Species: 10116 (Rattus norvegicus) [Search protein sequence]
HNVLMRLVASAYSIAQKAGTIVRCVIAEGDLGIVQKTSATDLQTKADRMV
QMSICSSLSRKFPKLTIIGEEDLPEVDQELIEDGQSEEILKQPCPSQYSA
IKEEDLVVWVDPVDGTKEYTEGLLDNVTVLIGIAYEGKAIAGIINQPYYN
YQAGPDAVLGRTIWGVLGLGAFGFQLKEAPAGKHIITTTRSHSNKLVTDC
IAAMNPDNVLRVGGAGNKIIQLIEGKASAYVFASPGCKKWDTCAPEVILH
AVGGKLTDIHGNPLQYDKEVKHMNSAGVLAALRNYEYYASRVPESVKSAL
IP
3D structure
PDB1jp4 Crystal structure of an enzyme displaying both inositol-polyphosphate-1-phosphatase and 3'-phosphoadenosine-5'-phosphate phosphatase activities: a novel target of lithium therapy.
ChainA
Resolution1.69 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D51 E74 D117 V119 D120 T122 D247
Catalytic site (residue number reindexed from 1) D47 E70 D111 V113 D114 T116 D241
Enzyme Commision number 3.1.3.57: inositol-1,4-bisphosphate 1-phosphatase.
3.1.3.7: 3'(2'),5'-bisphosphate nucleotidase.
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 PO4 A E74 D117 V119 D120 G121 T122 E70 D111 V113 D114 G115 T116
BS02 MG A D117 D120 D247 D111 D114 D241
BS03 MG A E74 D117 V119 E70 D111 V113
BS04 AMP A D120 T195 H198 G219 G220 K224 F238 G242 C243 D247 D114 T189 H192 G213 G214 K218 F232 G236 C237 D241
Gene Ontology
Molecular Function
GO:0000287 magnesium ion binding
GO:0004441 inositol-1,4-bisphosphate 1-phosphatase activity
GO:0008441 3'(2'),5'-bisphosphate nucleotidase activity
GO:0016787 hydrolase activity
GO:0046872 metal ion binding
Biological Process
GO:0008150 biological_process
GO:0046854 phosphatidylinositol phosphate biosynthetic process

View graph for
Molecular Function

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Biological Process
External links
PDB RCSB:1jp4, PDBe:1jp4, PDBj:1jp4
PDBsum1jp4
PubMed11812139
UniProtQ9Z1N4|BPNT1_RAT 3'(2'),5'-bisphosphate nucleotidase 1 (Gene Name=Bpnt1)

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