Structure of PDB 3qw2 Chain B

Receptor sequence

>3qw2B (length=392) Species: 2234 (Archaeoglobus fulgidus)

MKVWLVGAYGIVSTTAMVGARAIERGIAPKIGLVSELPHFEGIEKYAPFS
FEFGGHEIRLLSNAYEAAKEHWELNRHFDREILEAVKSDLEGIVARKGTA
LNCGSGIKELGDIKTLEGEGLSLAEMVSRIEEDIKSFADDETVVINVAST
EPLPNYSEEYHGSLEGFERMIDEDRKEYASASMLYAYAALKLGLPYANFT
PSPGSAIPALKELAEKKGVPHAGNDGKTGETLVKTTLAPMFAYRNMEVVG
WMSYAILGDYDGKVLSARDNKESKVLSKDKVLEKMLGYSPYSITEIQYFP
SLVDNKTAFDFVHFKGFLGKLMKFYFIWDAIDAIVAAPLILDIARFLLFA
KKKGVKGVVKEMAFFFKSPMDTNVINTHEQFVVLKEWYSNLK

3D structure

• PDB: 3qw2 Crystal structure of a trapped catalytic intermediate suggests that forced atomic proximity drives the catalysis of mIPS.
• Chain: B
• Resolution: 2.59 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): D225 K274 K306 K367
• 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

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	B	T228 G229 E230 T231 K306 K367	T228 G229 E230 T231 K306 K367
BS02	NAD	B	G7 G10 I11 V12 E57 I58 R59 T99 L110 V147 A148 S149 T150 Y185 F199 D225 G226 T228 D261 D332 A336	G7 G10 I11 V12 E57 I58 R59 T99 L110 V147 A148 S149 T150 Y185 F199 D225 G226 T228 D261 D332 A336

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

External links

• PDB: RCSB:3qw2, PDBe:3qw2, PDBj:3qw2
• PDBsum: 3qw2
• PubMed: 22261071
• UniProt: O28480