Brand  (β version)

PDB ID: 3CHP

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Ligands
Code Name Style Show Link
4BO (3s)-3-amino-4-oxo-4-[(4-phenylmethoxyphenyl)amino]butanoic acid PoSSuM
ACT Acetate ion PoSSuM
IMD Imidazole PoSSuM
YB Ytterbium (III) ion PoSSuM
ZN Zinc ion PoSSuM
Non-standard Residues
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Structure summary

Code : 3CHP   PDBj   RCSB PDB   PDBe
Header : HYDROLASE
Title : Crystal structure of leukotriene a4 hydrolase in complex with (3S)-3-amino-4-oxo-4-[(4-phenylmethoxyphenyl)amino]butanoic acid
Release Data : 2008-04-22
Compound :
mol_id molecule chains synonym
1 Leukotriene A-4 hydrolase A LTA-4 hydrolase, Leukotriene A(4) hydrolase
ec: 3.3.2.6
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: PT3-MB4
Authors : Thunnissen, M.M.G.M., Adler, M., Whitlow, M.
Keywords : EPOXIDE HYDROLASE, ALPHA-BETA PROTEIN, LEUKOTRIENE BIOSYNTHESIS, METALLOPROTEASE, Inhibitor complex, Alternative splicing, Cytoplasm, Metal-binding, Multifunctional enzyme, Zinc, HYDROLASE
Exp. method : X-RAY DIFFRACTION ( 2.10 Å )
Citation :

Synthesis of glutamic acid analogs as potent inhibitors of leukotriene A4 hydrolase.

Kirkland, T.A.,Adler, M.,Bauman, J.G.  et al.
(2008)  Bioorg.Med.Chem.  16 : 4963 - 4983

PubMed: 18394906
DOI: 10.1016/j.bmc.2008.03.042

Crystal Structure of Human Leukotriene A4 Hydrolase, a Bifunctional Enzyme in Inflammation

Thunnissen, M.M.G.M.,Nordlund, P.N.,Haeggstrom, J.Z.
(2001)  Nat.Struct.Biol.  8 : 131 - 135

Crystal structures of LEUKOTRIENE A4 HYDROLASE in complex with captopril and two competitive tight-binding inhibitors.

Thunnissen, M.M.G.M.,Anderson, B.,Samuelsson, B.  et al.
(2002)  FASEB J.  16 : 1648 - 1650

Leukotriene A4 Hydrolase: Selective Abrogation of Leukotriene B4 Formation by Mutation of Aspartic Acid 375.

Rudberg, P.C.,Tholander, F.,Thunnissen, M.M.  et al.
(2002)  Proc.Natl.Acad.Sci.USA  99 : 4215 - 4220

Leukotriene A4 Hydrolase: Identification of a Common Carboxylate Recognition Site for the Epoxide Hydrolase and Aminopeptidase Substrates

Rudberg, P.C.,Tholander, F.O.T.,Andberg, M.  et al.
(2004)  J.Mol.Biol.  279 : 27376 - 27382

Reaction

Chain : A
UniProt : P09960 (LKHA4_HUMAN)
Reaction: EC: Evidence:
Physiological Direction:
H2O + leukotriene A4 = 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
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