Structure of PDB 5ni2 Chain A

Receptor sequence
>5ni2A (length=607) Species: 9606 (Homo sapiens) [Search protein sequence]
IVDTCSLASPASVCRTKHLHLRCSVDFTRRTLTGTAALTVQSQEDNLRSL
VLDTKDLTIEKVVINGQEVKYALGERQSYKGSPMEISLPIALSKNQEIVI
EISFETSPKSSALQWLTPEQTSGKEHPYLFSQCQAIHCRAILPCQDTPSV
KLTYTAEVSVPKELVALMSAIRDGETPDPEDPSRKIYKFIQKVPIPCYLI
ALVVGALESRQIGPRTLVWSEKEQVEKSAYEFSETESMLKIAEDLGGPYV
WGQYDLLVLPPSFPYGGMANPCLTFVTPTLLAGDKSLSNVIAHEISHSWT
GNLVTNKTWDHFWLNEGHTVYLERHICGRLFGEKFRHFNALGGWGELQNS
VKTFGETHPFTKLVVDLTDIDPDVAYSSVPYEKGFALLFYLEQLLGGPEI
FLGFLKAYVEKFSYKSITTDDWKDFLYSYFKDKVDVLNQVDWNAWLYSPG
LPPIKPNYDMTLTNACIALSQRWITAKEDDLNSFNATDLKDLSSHQLNEF
LAQTLQRAPLPLGHIKRMQEVYNFNAINNSEIRFRWLRLCIQSKWEDAIP
LALKMATEQGRMKFTRPLFKDLAAFDKSHDQAVRTYQEHKASMHPVTAML
VGKDLKV
3D structure
PDB5ni2 Capturing LTA4 hydrolase in action: Insights to the chemistry and dynamics of chemotactic LTB4 synthesis.
ChainA
Resolution1.501 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) A271 H295 E296 H299 E318 D375 Y383
Catalytic site (residue number reindexed from 1) A269 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 H295 H299 E318 H293 H297 E316
BS02 DJ3 A Q136 A137 Y267 G268 G269 E296 F314 A377 Y378 Y383 R563 Q134 A135 Y265 G266 G267 E294 F312 A375 Y376 Y381 R561
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:5ni2, PDBe:5ni2, PDBj:5ni2
PDBsum5ni2
PubMed28827365
UniProtP09960|LKHA4_HUMAN Leukotriene A-4 hydrolase (Gene Name=LTA4H)

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