Structure of PDB 1p1j Chain A

Receptor sequence
>1p1jA (length=525) Species: 4932 (Saccharomyces cerevisiae) [Search protein sequence]
ITSVKVVTDKCTYKDNELLTKYSYENAVVTKTASGRFDVTPTVQDYVFKL
DLKKPEKLGIMLIGLGGNNGSTLVASVLANKHNVEFQTKEGVKQPNYFGS
MTQCSTLKLGIDAEGNDVYAPFNSLLPMVSPNDFVVSGWDINNADLYEAM
QRSQVLEYDLQQRLKAKMSLVKPLPSIYYPDFIAANQDERANNCINLDEK
GNVTTRGKWTHLQRIRRDIQNFKEENALDKVIVLWTANTERYVEVSPGVN
DTMENLLQSIKNDHEEIAPSTIFAAASILEGVPYINGSPQNTFVPGLVQL
AEHEGTFIAGDDLKSGQTKLKSVLAQFLVDAGIKPVSIASYNHLGNNDGY
NLSAPKQFRSKEISKSSVIDDIIASNDILYNDKLGKKVDHCIVIKYMKPV
GDSKVAMDEYYSELMLGGHNRISIHNVCEDSLLATPLIIDLLVMTEFCTR
VSYKKVDPVKEDAGKFENFYPVLTFLSYWLKAPLTRPGFHPVNGLNKQRT
ALENFLRLLIGLPSQNELRFEERLL
3D structure
PDB1p1j Structures of NAD(+)- and NADH-bound 1-l-myo-inositol 1-phosphate synthase.
ChainA
Resolution1.7 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D320 K369 K412 K489
Catalytic site (residue number reindexed from 1) D312 K361 K404 K481
Enzyme Commision number 5.5.1.4: inositol-3-phosphate synthase.
Interaction with ligand
Gene Ontology
Molecular Function
GO:0004512 inositol-3-phosphate synthase activity
GO:0016853 isomerase activity
Biological Process
GO:0006021 inositol biosynthetic process
GO:0008654 phospholipid biosynthetic process
Cellular Component
GO:0005737 cytoplasm

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Molecular Function

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Biological Process

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Cellular Component
External links
PDB RCSB:1p1j, PDBe:1p1j, PDBj:1p1j
PDBsum1p1j
PubMed12832758
UniProtP11986|INO1_YEAST Inositol-3-phosphate synthase (Gene Name=INO1)

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