Brand  (β version)

PDB ID: 5NI2

Hetero Atom Contents

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Code Name Style Show Link
DJ3 5s-5,6-oxido-7,9-trans-11,14-cis-eicosatetraenoic acid PoSSuM
YB Ytterbium (III) ion PoSSuM
ZN Zinc ion PoSSuM

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Structure summary

Code : 5NI2   PDBj   RCSB PDB   PDBe
Header : HYDROLASE
Title : Crystal structure of human LTA4H mutant E271A in complex with LTA4 (crystal form I)
Release Data : 2017-08-23
Compound :
mol_id molecule chains synonym
1 Leukotriene A-4 hydrolase A LTA-4 hydrolase,Leukotriene A(4) hydrolase
ec: 3.3.2.6
mutation: E271A
Source :
mol_id organism_scientific organism_common expression_system
1 Homo sapiens  (taxid:9606) Human Escherichia coli  (taxid:562)
gene: LTA4H, LTA4
expression_system_strain: JM101
expression_system_vector_type: plasmid
expression_system_plasmid: pT3MB4
Authors : Stsiapanava, A.
Keywords : Metallopeptidase, epoxide hydrolase, leukotriene A4, hydrolase
Exp. method : X-RAY DIFFRACTION ( 1.501 Å )
Citation :

Capturing LTA4 hydrolase in action: Insights to the chemistry and dynamics of chemotactic LTB4 synthesis.

Stsiapanava, A.,Samuelsson, B.,Haeggstrom, J.Z.
(2017)  Proc. Natl. Acad. Sci. U.S.A.  114 : 9689 - 9694

PubMed: 28827365
DOI: 10.1073/pnas.1710850114

Reaction

Chain : A
UniProt : P09960 (LKHA4_HUMAN)
Reaction: EC: Evidence:
Physiological Direction:
leukotriene A4 + H2O = leukotriene B4 3.3.2.6 PubMed:11675384, PubMed:11917124, PubMed:12207002, PubMed:15078870, PubMed:18804029, PubMed:1897988, PubMed:24591641, PubMed:6490615, PubMed:7667299, PubMed:9395533
left-to-right PubMed:11917124
(5S,6S)-epoxy-(18R)-hydroxy-(7E,9E,11Z,14Z,16E)- eicosapentaenoate + H2O = resolvin E1 - PubMed:21206090
left-to-right
(5S,6S)-epoxy-(18S)-hydroxy-(7E,9E,11Z,14Z,16E)- eicosapentaenoate + H2O = 18S-resolvin E1 - PubMed:21206090
left-to-right
Release of the N-terminal residue from a tripeptide. 3.4.11.4 PubMed:11675384, PubMed:11917124, PubMed:20813919, PubMed:24591641, PubMed:9395533
-
leukotriene A5 + H2O = leukotriene B5 - PubMed:2996528
left-to-right
Cofactor: Evidence: Note:
Zn(2+) ECO:0000269 | PubMed:11175901
ECO:0000269 | PubMed:12207002
ECO:0000269 | PubMed:15078870
ECO:0000269 | PubMed:18804029
ECO:0000269 | PubMed:24591641
Binds 1 zinc ion per subunit.