Structure of PDB 5mef Chain A

Receptor sequence
>5mefA (length=569) Species: 41431 (Rippkaea orientalis PCC 8801) [Search protein sequence]
MVQPSLPQDDTPDQQEQRNRAIAQQREAYQYSETAGILLIKTLPQSEMFS
LKYLIERDKGLVSLIANTLASNIENIFDPFDKLEDFEEMFPLLPKPLVMN
TFRNDRVFARQRIAGPNPMVIERVVDKLPDNFPVTDAMFQKIMFTKKTLA
EAIAQGKLFITNYKGLAELSPGRYEYQKNGTLVQKTKTIAAPLVLYAWKP
EGFGDYRGSLAPIAIQINQQPDPITNPIYTPRDGKHWFIAKIFAQMADGN
CHEAISHLARTHLILEPFVLATANELAPNHPLSVLLKPHFQFTLAINELA
REQFISAGGYADDLLAGTLEASIAVIKAAIKEYMDNFTEFALPRELARRG
VGIGDVDQRGENFLPDYPYRDDAMLLWNAIEVYVRDYLSLYYQSPVQIRQ
DTELQNWVRRLVSPEGGRVTGLVSNGELNTIEALVAIATQVIFVSGPQHA
AVNYPQYDYMAFIPNMPLATYATPPNKESNISEATILNILPPQKLAARQL
ELMRTLCVFYPNRLGYPDTEFVDVRAQQVLHQFQERLQEIEQRIVLCNEK
RLEPYTYLLPSNVPNSTSI
3D structure
PDB5mef Lipoxygenase 2 from Cyanothece sp. controls dioxygen insertion by steric shielding and substrate fixation.
ChainA
Resolution2.357 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H257 H262 H449 N453 I569
Catalytic site (residue number reindexed from 1) H257 H262 H449 N453 I569
Enzyme Commision number 1.13.11.33: arachidonate 15-lipoxygenase.
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 FE A H257 H262 H449 N453 I569 H257 H262 H449 N453 I569
Gene Ontology
Molecular Function
GO:0016491 oxidoreductase activity
GO:0016702 oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen
GO:0046872 metal ion binding
GO:0050473 arachidonate 15-lipoxygenase activity
Biological Process
GO:0034440 lipid oxidation

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Molecular Function
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Biological Process
External links
PDB RCSB:5mef, PDBe:5mef, PDBj:5mef
PDBsum5mef
PubMed28522865
UniProtB7JX99

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