Structure of PDB 3fum Chain A

Receptor sequence
>3fumA (length=605) Species: 9606 (Homo sapiens) [Search protein sequence]
DTCSLASPASVCRTKHLHLRCSVDFTRRTLTGTAALTVQSQEDNLRSLVL
DTKDLTIEKVVINGQEVKYALGERQSYKGSPMEISLPIALSKNQEIVIEI
SFETSPKSSALQWLTPEQTSGKEHPYLFSQCQAIHCRAILPCQDTPSVKL
TYTAEVSVPKELVALMSAIRDGETPDPEDPSRKIYKFIQKVPIPCYLIAL
VVGALESRQIGPRTLVWSEKEQVEKSAYEFSETESMLKIAEDLGGPYVWG
QYDLLVLPPSFPYGGMENPCLTFVTPTLLAGDKSLSNVIAHEISHSWTGN
LVTNKTWDHFWLNEGHTVYLERHICGRLFGEKFRHFNALGGWGELQNSVK
TFGETHPFTKLVVDLTDIDPDVAYSSVPYEKGFALLFYLEQLLGGPEIFL
GFLKAYVEKFSYKSITTDDWKDFLYSYFKDKVDVLNQVDWNAWLYSPGLP
PIKPNYDMTLTNACIALSQRWITAKEDDLNSFNATDLKDLSSHQLNEFLA
QTLQRAPLPLGHIKRMQEVYNFNAINNSEIRFRWLRLCIQSKWEDAIPLA
LKMATEQGRMKFTRPLFKDLAAFDKSHDQAVRTYQEHKASMHPVTAMLVG
KDLKV
3D structure
PDB3fum Discovery of leukotriene A4 hydrolase inhibitors using metabolomics biased fragment crystallography.
ChainA
Resolution2.15 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) E267 H291 E292 H295 E314 D371 Y379
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 ZN A H295 H299 E318 H291 H295 E314
BS02 80A A Q136 A137 Y267 G269 M270 W311 F314 V367 L369 P374 A377 Y378 Y383 Q132 A133 Y263 G265 M266 W307 F310 V363 L365 P370 A373 Y374 Y379 MOAD: ic50=170uM
PDBbind-CN: -logKd/Ki=3.77,IC50=170uM
BindingDB: IC50=202000nM
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:3fum, PDBe:3fum, PDBj:3fum
PDBsum3fum
PubMed19618939
UniProtP09960|LKHA4_HUMAN Leukotriene A-4 hydrolase (Gene Name=LTA4H)

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