Structure of PDB 1u1i Chain D

Receptor sequence
>1u1iD (length=392) Species: 224325 (Archaeoglobus fulgidus DSM 4304) [Search protein sequence]
MKVWLVGAYGIVSTTAMVGARAIERGIAPKIGLVSELPHFEGIEKYAPFS
FEFGGHEIRLLSNAYEAAKEHWELNRHFDREILEAVKSDLEGIVARKGTA
LNCGSGIKELGDIKTLEGEGLSLAEMVSRIEEDIKSFADDETVVINVAST
EPLPNYSEEYHGSLEGFERMIDEDRKEYASASMLYAYAALKLGLPYANFT
PSPGSAIPALKELAEKKGVPHAGNDGKTGETLVKTTLAPMFAYRNMEVVG
WMSYNILGDYDGKVLSARDNKESKVLSKDKVLEKMLGYSPYSITEIQYFP
SLVDNKTAFDFVHFKGFLGKLMKFYFIWDAIDAIVAAPLILDIARFLLFA
KKKGVKGVVKEMAFFFKSPMDTNVINTHEQFVVLKEWYSNLK
3D structure
PDB1u1i Reaching for Mechanistic Consensus Across Life Kingdoms: Structure and Insights into Catalysis of the myo-Inositol-1-phosphate Synthase (mIPS) from Archaeoglobus fulgidus
ChainD
Resolution1.9 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D1425 K1474 K1506 K1567
Catalytic site (residue number reindexed from 1) D225 K274 K306 K367
Enzyme Commision number 5.5.1.4: inositol-3-phosphate synthase.
Interaction with ligand
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0004512 inositol-3-phosphate synthase activity
Biological Process
GO:0006021 inositol biosynthetic process
GO:0006629 lipid metabolic process
GO:0008654 phospholipid biosynthetic process
Cellular Component
GO:0005737 cytoplasm
GO:0016020 membrane

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Molecular Function

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Biological Process

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Cellular Component
External links
PDB RCSB:1u1i, PDBe:1u1i, PDBj:1u1i
PDBsum1u1i
PubMed15628862
UniProtO28480

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