Structure of PDB 1cqe Chain A

Receptor sequence

>1cqeA (length=552) Species: 9940 (Ovis aries)

PVNPCCYYPCQHQGICVRFGLDRYQCDCTRTGYSGPNCTIPEIWTWLRTT
LRPSPSFIHFLLTHGRWLWDFVNATFIRDTLMRLVLTVRSNLIPSPPTYN
IAHDYISWESFSNVSYYTRILPSVPRDCPTPMGTKGKKQLPDAEFLSRRF
LLRRKFIPDPQGTNLMFAFFAQHFTHQFFKTSGKMGPGFTKALGHGVDLG
HIYGDNLERQYQLRLFKDGKLKYQMLNGEVYPPSVEEAPVLMHYPRGIPP
QSQMAVGQEVFGLLPGLMLYATIWLREHNRVCDLLKAEHPTWGDEQLFQT
ARLILIGETIKIVIEEYVQQLSGYFLQLKFDPELLFGAQFQYRNRIAMEF
NQLYHWHPLMPDSFRVGPQDYSYEQFLFNTSMLVDYGVEALVDAFSRQPA
GRIGGGRNIDHHILHVAVDVIKESRVLRLQPFNEYRKRFGMKPYTSFQEL
TGEKEMAAELEELYGDIDALEFYPGLLLEKCHPNSIFGESMIEMGAPFSL
KGLLGNPICSPEYWKASTFGGEVGFNLVKTATLKKLVCLNTKTCPYVSFH
VP

3D structure

• PDB: 1cqe The X-ray crystal structure of the membrane protein prostaglandin H2 synthase-1.
• Chain: A
• Resolution: 3.1 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): Q203 H207 L384 Y385 H388 G526 S530
• Catalytic site (residue number reindexed from 1): Q172 H176 L353 Y354 H357 G495 S499
• Enzyme Commision number: 1.14.99.1: prostaglandin-endoperoxide 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	HEM	A	A202 Q203 H207 F210 K211 T212 L295 N382 Y385 H386 H388 M391 V447 D450	A171 Q172 H176 F179 K180 T181 L264 N351 Y354 H355 H357 M360 V416 D419
BS02	FLP	A	R120 V349 L352 Y355 Y385 W387 G526 A527 S530	R89 V318 L321 Y324 Y354 W356 G495 A496 S499	BindingDB: IC50=150nM,Ki=1000nM

Gene Ontology

Molecular Function

• GO:0004601 peroxidase activity
• GO:0020037 heme binding

Biological Process

• GO:0006979 response to oxidative stress

External links

• PDB: RCSB:1cqe, PDBe:1cqe, PDBj:1cqe
• PDBsum: 1cqe
• PubMed: 8121489
• UniProt: P05979|PGH1_SHEEP Prostaglandin G/H synthase 1 (Gene Name=PTGS1)