Structure of PDB 4fm5 Chain D

Receptor sequence
>4fm5D (length=552) Species: 10090 (Mus musculus) [Search protein sequence]
ANPCCSNPCQNRGECMSTGFDQYKCDCTRTGFYGENCTTPEFLTRIKLLL
KPTPNTVHYILTHFKGVWNIVNNIPFLRSLIMKYVLTSRSYLIDSPPTYN
VHYGYKSWEAFSNLSYYTRALPPVADDCPTPMGVKGNKELPDSKEVLEKV
LLRREFIPDPQGSNMMFAFFAQHFTHQFFKTDHKRGPGFTRGLGHGVDLN
HIYGETLDRQHKLRLFKDGKLKYQVIGGEVYPPTVKDTQVEMIYPPHIPE
NLQFAVGQEVFGLVPGLMMYATIWLREHNRVCDILKQEHPEWGDEQLFQT
SRLILIGETIKIVIEDYVQHLSGYHFKLKFDPELLFNQQFQYQNRIASEF
NTLYHWHPLLPDTFNIEDQEYSFKQFLYNNSILLEHGLTQFVESFTRQIA
GRVAGGRNVPIAVQAVAKASIDQSREMKYQSLNEYRKRFSLKPYTSFEEL
TGEKEMAAELKALYSDIDVMELYPALLVEKPRPDAIFGETMVELGAPFSL
KGLMGNPICSPQYWKPSTFGGEVGFKIINTASIQSLICNNVKGCPFTSFN
VQ
3D structure
PDB4fm5 Substrate-Selective Inhibition of Cyclooxygenase-2: Development and Evaluation of Achiral Profen Probes.
ChainD
Resolution2.81 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) 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 Q203 H207 F210 K211 T212 H214 Y385 H386 W387 H388 L391 F395 Q172 H176 F179 K180 T181 H183 Y354 H355 W356 H357 L360 F364
BS02 DF0 D R120 V349 L352 Y355 Y385 W387 G526 A527 S530 R89 V318 L321 Y324 Y354 W356 G495 A496 S499 BindingDB: IC50=110nM
Gene Ontology
Molecular Function
GO:0004601 peroxidase activity
GO:0020037 heme binding
Biological Process
GO:0006979 response to oxidative stress

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Molecular Function
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Biological Process
External links
PDB RCSB:4fm5, PDBe:4fm5, PDBj:4fm5
PDBsum4fm5
PubMed22984634
UniProtQ05769|PGH2_MOUSE Prostaglandin G/H synthase 2 (Gene Name=Ptgs2)

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