Structure of PDB 4rsy Chain A

Receptor sequence
>4rsyA (length=607) Species: 9606 (Homo sapiens) [Search protein sequence]
VDTCSLASPASVCRTKHLHLRCSVDFTRRTLTGTAALTVQSQEDNLRSLV
LDTKDLTIEKVVINGQEVKYALGERQSYKGSPMEISLPIALSKNQEIVIE
ISFETSPKSSALQWLTPEQTSGKEHPYLFSQCQAIHCRAILPCQDTPSVK
LTYTAEVSVPKELVALMSAIRDGETPDPEDPSRKIYKFIQKVPIPCYLIA
LVVGALESRQIGPRTLVWSEKEQVEKSAYEFSETESMLKIAEDLGGPYVW
GQYDLLVLPPSFPYGGMENPCLTFVTPTLLAGDKSLSNVIAHEISHSWTG
NLVTNKTWDHFWLNEGHTVYLERHICGRLFGEKFRHFNALGGWGELQNSV
KTFGETHPFTKLVVDLTDIDPDVAYSSVPYEKGFALLFYLEQLLGGPEIF
LGFLKAYVEKFSYKSITTDDWKDFLYSYFKDKVDVLNQVDWNAWLYSPGL
PPIKPNYDMTLTNACIALSQRWITAKEDDLNSFNATDLKDLSSHQLNEFL
AQTLQRAPLPLGHIKRMQEVYNFNAINNSEIRFRWLRLCIQSKWEDAIPL
ALKMATEQGRMKFTRPLFKDLAAFDKSHDQAVRTYQEHKASMHPVTAMLV
GKDLKVD
3D structure
PDB4rsy Structure of Human Leukotriene A4 Hydrolase in complex with inhibitor H1
ChainA
Resolution1.93 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) E271 H295 E296 H299 E318 D375 Y383
Catalytic site (residue number reindexed from 1) E268 H292 E293 H296 E315 D372 Y380
Enzyme Commision number 3.3.2.6: leukotriene-A4 hydrolase.
3.4.11.4: tripeptide aminopeptidase.
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 B3N A Q136 A137 Y267 G269 H295 E296 H299 W311 F314 E318 P374 A377 Y378 Y383 Q133 A134 Y264 G266 H292 E293 H296 W308 F311 E315 P371 A374 Y375 Y380 BindingDB: IC50=300nM
BS02 ZN A H295 H299 E318 H292 H296 E315
Gene Ontology
Molecular Function
GO:0003723 RNA binding
GO:0004177 aminopeptidase activity
GO:0004301 epoxide hydrolase activity
GO:0004463 leukotriene-A4 hydrolase activity
GO:0005515 protein binding
GO:0008233 peptidase activity
GO:0008237 metallopeptidase activity
GO:0008270 zinc ion binding
GO:0045148 tripeptide aminopeptidase activity
GO:0046872 metal ion binding
GO:0070006 metalloaminopeptidase activity
Biological Process
GO:0006508 proteolysis
GO:0006629 lipid metabolic process
GO:0006691 leukotriene metabolic process
GO:0010043 response to zinc ion
GO:0019370 leukotriene biosynthetic process
GO:0019538 protein metabolic process
GO:0043171 peptide catabolic process
GO:0043434 response to peptide hormone
GO:0060509 type I pneumocyte differentiation
Cellular Component
GO:0005576 extracellular region
GO:0005634 nucleus
GO:0005654 nucleoplasm
GO:0005737 cytoplasm
GO:0005829 cytosol
GO:0070062 extracellular exosome
GO:1904724 tertiary granule lumen
GO:1904813 ficolin-1-rich granule lumen

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:4rsy, PDBe:4rsy, PDBj:4rsy
PDBsum4rsy
PubMed
UniProtP09960|LKHA4_HUMAN Leukotriene A-4 hydrolase (Gene Name=LTA4H)

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