Structure of PDB 5med Chain B

Receptor sequence
>5medB (length=565) Species: 41431 (Rippkaea orientalis PCC 8801) [Search protein sequence]
MVQPSLPQDDTPDQQEQRNRAIAQQREAYQYSETAGILLIKTLPQSEMFS
LKYLIERDKGLVSLIANTLASNIENIFDPFDKLEDFEEMFPLLPKPLVMN
TFRNDRVFARQRIAGPNPMVIERVVDKLPDNFPVTDAMFQKIMFTKKTLA
EAIAQGKLFITNYKGLAELSPGRYEYQKNGTLVQKTKTIAAPLVLYAWKP
EGRGSLAPIAIQINQQPDPITNPIYTPRDGKHWFIAKIFAQMADGNCHEA
ISHLARTHLILEPFVLATANELAPNHPLSVLLKPHFQFTLAINELAREQL
ISAGGYADDLLAGTLEASIAVIKAAIKEYMDNFTEFALPRELARRGVGIG
DVDQRGENFLPDYPYRDDAMLLWNAIEVYVRDYLSLYYQSPVQIRQDTEL
QNWVRRLVSPEGGRVTGLVSNGELNTIEALVAIATQVIFVSGPQHAAVNY
PQYDYMAFIPNMPLATYATPPNKESNISEATILNILPPQKLAARQLELMR
TLCVFYPNRLGYPDTEFVDVRAQQVLHQFQERLQEIEQRIVLCNEKRLEP
YTYLLPSNVPNSTSI
3D structure
PDB5med Lipoxygenase 2 from Cyanothece sp. controls dioxygen insertion by steric shielding and substrate fixation.
ChainB
Resolution1.8 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) H253 H258 H445 N449 I565
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 B H257 H262 H449 N453 I569 H253 H258 H445 N449 I565
BS02 POL B H262 I296 L299 A300 H258 I292 L295 A296
BS03 PDO B Q45 S46 Q45 S46
BS04 PDO B G417 R418 G413 R414
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:5med, PDBe:5med, PDBj:5med
PDBsum5med
PubMed28522865
UniProtB7JX99

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