Structure of PDB 1la2 Chain D

Receptor sequence
>1la2D (length=514) Species: 4932 (Saccharomyces cerevisiae) [Search protein sequence]
TSVKVVTDKCTYKDNELLTKYSYENAVVTKTASGRFDVTPTVQDYVFKLD
LKKPEKLGIMLIGLGGNNGSTLVASVLANKHNVEFQTKEGVKQPNYFGSM
TQCSTLKLGIDAEGNDVYAPFNSLLPMVSPNDFVVSGWDINNADLYEAMQ
RSQVLEYDLQQRLKAKMSLVKPLPSIYYPDFIAANQDERANNCINLDEKG
NVTTRGKWTHLQRIRRDIQNFKEENALDKVIVLWTANTERYVEVSPGVND
TMENLLQSIKNDHEEIAPSTIFAAASILEGVPYINGSPQNTFVPGLVQLA
EHEGTFIAGDDLKSGQTKLKSVLAQFLVDAGIKPVSIASYNHLGNNDGYN
LSAPKSVIDDIIASNDILYNDKLGKKVDHCIVIKYMKPVGDSKVAMDEYY
SELMLGGHNRISIHNVCEDSLLATPLIIDLLVMTEFCTRVSYKKVDPVKE
DAGKFENFYPVLTFLSYWLKAPLTRPGFHPVNGLNKQRTALENFLRLLIG
LPSQNELRFEERLL
3D structure
PDB1la2 Structural analysis of Saccharomyces cerevisiae myo-inositol phosphate synthase
ChainD
Resolution2.65 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 K412 K489
Catalytic site (residue number reindexed from 1) D311 K393 K470
Enzyme Commision number 5.5.1.4: inositol-3-phosphate synthase.
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 NAD D G75 N76 N77 D148 I149 S184 I185 R198 T244 A245 N246 T247 G295 L321 N355 D356 D438 A442 G66 N67 N68 D139 I140 S175 I176 R189 T235 A236 N237 T238 G286 L312 N346 D347 D419 A423
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:1la2, PDBe:1la2, PDBj:1la2
PDBsum1la2
PubMed12836703
UniProtP11986|INO1_YEAST Inositol-3-phosphate synthase (Gene Name=INO1)

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