Structure of PDB 1pxx Chain D

Receptor sequence
>1pxxD (length=552) Species: 10090 (Mus musculus) [Search protein sequence]
ANPCCSNPCQNRGECMSTGFDQYKCDCTRTGFYGENCTTPEFLTRIKLLL
KPTPNTVHYILTHFKGVWNIVNNIPFLRSLIMKYVLTSRSYLIDSPPTYN
VHYGYKSWEAFSNLSYYTRALPPVADDCPTPMGVKGNKELPDSKEVLEKV
LLRREFIPDPQGSNMMFAFFAQHFTHQFFKTDHKRGPGFTRGLGHGVDLN
HIYGETLDRQHKLRLFKDGKLKYQVIGGEVYPPTVKDTQVEMIYPPHIPE
NLQFAVGQEVFGLVPGLMMYATIWLREHNRVCDILKQEHPEWGDEQLFQT
SRLILIGETIKIVIEDYVQHLSGYHFKLKFDPELLFNQQFQYQNRIASEF
NTLYHWHPLLPDTFNIEDQEYSFKQFLYNNSILLEHGLTQFVESFTRQIA
GRVAGGRNVPIAVQAVAKASIDQSREMKYQSLNEYRKRFSLKPYTSFEEL
TGEKEMAAELKALYSDIDVMELYPALLVEKPRPDAIFGETMVELGAPFSL
KGLMGNPICSPQYWKPSTFGGEVGFKIINTASIQSLICNNVKGCPFTSFN
VQ
3D structure
PDB1pxx A Novel Mechanism of Cyclooxygenase-2 Inhibition Involving Interactions with Ser-530 and Tyr-385.
ChainD
Resolution2.9 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) Q3203 H3207 L3384 Y3385 H3388 G3526 S3530
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 D Q3203 H3207 F3210 T3212 Y3385 H3386 H3388 L3391 V3447 Q172 H176 F179 T181 Y354 H355 H357 L360 V416
BS02 DIF D Y3348 V3349 L3352 Y3385 W3387 V3523 G3526 A3527 S3530 Y317 V318 L321 Y354 W356 V492 G495 A496 S499 BindingDB: IC50=22nM
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:1pxx, PDBe:1pxx, PDBj:1pxx
PDBsum1pxx
PubMed12925531
UniProtQ05769|PGH2_MOUSE Prostaglandin G/H synthase 2 (Gene Name=Ptgs2)

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