Structure of PDB 1cqe Chain B

Receptor sequence
>1cqeB (length=553) Species: 9940 (Ovis aries) [Search protein sequence]
APVNPCCYYPCQHQGICVRFGLDRYQCDCTRTGYSGPNCTIPEIWTWLRT
TLRPSPSFIHFLLTHGRWLWDFVNATFIRDTLMRLVLTVRSNLIPSPPTY
NIAHDYISWESFSNVSYYTRILPSVPRDCPTPMGTKGKKQLPDAEFLSRR
FLLRRKFIPDPQGTNLMFAFFAQHFTHQFFKTSGKMGPGFTKALGHGVDL
GHIYGDNLERQYQLRLFKDGKLKYQMLNGEVYPPSVEEAPVLMHYPRGIP
PQSQMAVGQEVFGLLPGLMLYATIWLREHNRVCDLLKAEHPTWGDEQLFQ
TARLILIGETIKIVIEEYVQQLSGYFLQLKFDPELLFGAQFQYRNRIAME
FNQLYHWHPLMPDSFRVGPQDYSYEQFLFNTSMLVDYGVEALVDAFSRQP
AGRIGGGRNIDHHILHVAVDVIKESRVLRLQPFNEYRKRFGMKPYTSFQE
LTGEKEMAAELEELYGDIDALEFYPGLLLEKCHPNSIFGESMIEMGAPFS
LKGLLGNPICSPEYWKASTFGGEVGFNLVKTATLKKLVCLNTKTCPYVSF
HVP
3D structure
PDB1cqe The X-ray crystal structure of the membrane protein prostaglandin H2 synthase-1.
ChainB
Resolution3.1 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) Q203 H207 L384 Y385 H388 G526 S530
Catalytic site (residue number reindexed from 1) Q173 H177 L354 Y355 H358 G496 S500
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 B A202 Q203 H207 K211 T212 L295 N382 Y385 H386 H388 M391 V447 D450 A172 Q173 H177 K181 T182 L265 N352 Y355 H356 H358 M361 V417 D420
BS02 FLP B R120 V349 L352 Y355 Y385 W387 G526 A527 S530 R90 V319 L322 Y325 Y355 W357 G496 A497 S500 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

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:1cqe, PDBe:1cqe, PDBj:1cqe
PDBsum1cqe
PubMed8121489
UniProtP05979|PGH1_SHEEP Prostaglandin G/H synthase 1 (Gene Name=PTGS1)

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