Structure of PDB 1iuq Chain A

Receptor sequence

>1iuqA (length=357) Species: 3662 (Cucurbita moschata)

ASHSRKFLDVRSEEELLSCIKKETEAGKLPPNVAAGMEELYQNYRNAVIE
SGNPKADEIVLSNMTVALDRILLDVEDPFVFSSHHKAIREPFDYYIFGQN
YIRPLIDFGNSFVGNLSLFKDIEEKLQQGHNVVLISNHQTEADPAIISLL
LEKTNPYIAENTIFVAGDRVLADPLCKPFSIGRNLICVYSKKHMFDIPEL
TETKRKANTRSLKEMALLLRGGSQLIWIAPSGGRDRPDPSTGEWYPAPFD
ASSVDNMRRLIQHSDVPGHLFPLALLCHDIMPPPRVIAFNGAGLSVAPEI
SFEEIAATHKNPEEVREAYSKALFDSVAMQYNVLKTAISGKQGLGASTAD
VSLSQPW

3D structure

• PDB: 1iuq Substrate recognition and selectivity of plant glycerol-3-phosphate acyltransferases (GPATs) from Cucurbita moscata and Spinacea oleracea.
• Chain: A
• Resolution: 1.55 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): H139 D144
• Catalytic site (residue number reindexed from 1): H138 D143
• Enzyme Commision number: 2.3.1.15: glycerol-3-phosphate 1-O-acyltransferase.
  2.3.1.n5: glycerol-3-phosphate acyltransferase (acyl-[acyl-carrier-protein]- transferring).

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	GOL	A	L74 D75 D78 F80	L73 D74 D77 F79
BS02	GOL	A	L219 Q225	L218 Q224
BS03	GOL	A	P249 F250 E328 S331 F335	P248 F249 E317 S320 F324
BS04	GOL	A	E142 D169 R170 H194	E141 D168 R169 H193
BS05	GOL	A	Y246 A339	Y245 A328

Gene Ontology

Molecular Function

• GO:0004366 glycerol-3-phosphate O-acyltransferase activity
• GO:0016746 acyltransferase activity

Biological Process

• GO:0006650 glycerophospholipid metabolic process

External links

• PDB: RCSB:1iuq, PDBe:1iuq, PDBj:1iuq
• PDBsum: 1iuq
• PubMed: 14684887
• UniProt: P10349|GPAT2_CUCMO Glycerol-3-phosphate acyltransferase ATS12, chloroplastic (Gene Name=ATS1;2)