Structure of PDB 3b7s Chain A Binding Site BS01

Receptor Information
>3b7s Chain A (length=610) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
PEIVDTCSLASPASVCRTKHLHLRCSVDFTRRTLTGTAALTVQSQEDNLR
SLVLDTKDLTIEKVVINGQEVKYALGERQSYKGSPMEISLPIALSKNQEI
VIEISFETSPKSSALQWLTPEQTSGKEHPYLFSQCQAIHCRAILPCQDTP
SVKLTYTAEVSVPKELVALMSAIRDGETPDPEDPSRKIYKFIQKVPIPCY
LIALVVGALESRQIGPRTLVWSEKEQVEKSAYEFSETESMLKIAEDLGGP
YVWGQYDLLVLPPSFPYGGMENPCLTFVTPTLLAGDKSLSNVIAHQISHS
WTGNLVTNKTWDHFWLNEGHTVYLERHICGRLFGEKFRHFNALGGWGELQ
NSVKTFGETHPFTKLVVDLTDIDPDVAYSSVPYEKGFALLFYLEQLLGGP
EIFLGFLKAYVEKFSYKSITTDDWKDFLYSYFKDKVDVLNQVDWNAWLYS
PGLPPIKPNYDMTLTNACIALSQRWITAKEDDLNSFNATDLKDLSSHQLN
EFLAQTLQRAPLPLGHIKRMQEVYNFNAINNSEIRFRWLRLCIQSKWEDA
IPLALKMATEQGRMKFTRPLFKDLAAFDKSHDQAVRTYQEHKASMHPVTA
MLVGKDLKVD
Ligand information
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB3b7s Structure-based dissection of the active site chemistry of leukotriene a4 hydrolase: implications for m1 aminopeptidases and inhibitor design.
Resolution1.465 Å
Binding residue
(original residue number in PDB)		Q136 Y267 G268 G269 E271 H295 Q296 H299 E318 Y378 S380 Y383 R563
Binding residue
(residue number reindexed from 1)		Q136 Y267 G268 G269 E271 H295 Q296 H299 E318 Y378 S380 Y383 R563
Enzymatic activity
Catalytic site (original residue number in PDB) E271 H295 Q296 H299 E318 D375 Y383
Catalytic site (residue number reindexed from 1) E271 H295 Q296 H299 E318 D375 Y383
Enzyme Commision number 3.3.2.6: leukotriene-A4 hydrolase.
3.4.11.4: tripeptide aminopeptidase.
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:3b7s, PDBe:3b7s, PDBj:3b7s
PDBsum3b7s
PubMed18804029
UniProtP09960|LKHA4_HUMAN Leukotriene A-4 hydrolase (Gene Name=LTA4H)

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