Structure of PDB 3u9w Chain A

Receptor sequence
>3u9wA (length=608) Species: 9606 (Homo sapiens) [Search protein sequence]
IVDTCSLASPASVCRTKHLHLRCSVDFTRRTLTGTAALTVQSQEDNLRSL
VLDTKDLTIEKVVINGQEVKYALGERQSYKGSPMEISLPIALSKNQEIVI
EISFETSPKSSALQWLTPEQTSGKEHPYLFSQCQAIHCRAILPCQDTPSV
KLTYTAEVSVPKELVALMSAIRDGETPDPEDPSRKIYKFIQKVPIPCYLI
ALVVGALESRQIGPRTLVWSEKEQVEKSAYEFSETESMLKIAEDLGGPYV
WGQYDLLVLPPSFPYGGMENPCLTFVTPTLLAGDKSLSNVIAHEISHSWT
GNLVTNKTWDHFWLNEGHTVYLERHICGRLFGEKFRHFNALGGWGELQNS
VKTFGETHPFTKLVVDLTDIDPDVAYSSVPYEKGFALLFYLEQLLGGPEI
FLGFLKAYVEKFSYKSITTDDWKDFLYSYFKDKVDVLNQVDWNAWLYSPG
LPPIKPNYDMTLTNACIALSQRWITAKEDDLNSFNATDLKDLSSHQLNEF
LAQTLQRAPLPLGHIKRMQEVYNFNAINNSEIRFRWLRLCIQSKWEDAIP
LALKMATEQGRMKFTRPLFKDLAAFDKSHDQAVRTYQEHKASMHPVTAML
VGKDLKVD
3D structure
PDB3u9w Structure of human Leukotriene A4 hydrolase in complex with inhibitor sc57461A
ChainA
Resolution1.25 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) E1271 H1295 E1296 H1299 E1318 D1375 Y1383
Catalytic site (residue number reindexed from 1) E269 H293 E294 H297 E316 D373 Y381
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 H1295 H1299 E1318 H293 H297 E316
BS02 28P A Q1136 A1137 Y1267 G1269 M1270 E1271 H1295 E1296 H1299 W1311 F1314 E1318 P1374 A1377 Y1378 P1382 Y1383 Q134 A135 Y265 G267 M268 E269 H293 E294 H297 W309 F312 E316 P372 A375 Y376 P380 Y381 BindingDB: IC50=6.0nM,Kd=350nM,Ki=3.0nM
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:3u9w, PDBe:3u9w, PDBj:3u9w
PDBsum3u9w
PubMed
UniProtP09960|LKHA4_HUMAN Leukotriene A-4 hydrolase (Gene Name=LTA4H)

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