Target Binding Site Detail

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Target General Information
Ligand General Information
Drug Binding Sites of Target
References
Target General Information  Top
Target ID T72881 Target Info
Target Name Leukotriene C4 synthase (LTC4S)
Synonyms Leukotriene-C(4)Leukotriene C4 synthase synthase; Leukotriene-C(4) synthase; LTC4 synthase
Target Type Patented-recorded Target
Gene Name LTC4S
Biochemical Class Carbon-sulfur lyase
UniProt ID
LTC4S_HUMAN
Ligand General Information  Top
Ligand Name Glutathione Ligand Info
Canonical SMILES C(CC(=O)NC(CS)C(=O)NCC(=O)O)C(C(=O)O)N
InChI 1S/C10H17N3O6S/c11-5(10(18)19)1-2-7(14)13-6(4-20)9(17)12-3-8(15)16/h5-6,20H,1-4,11H2,(H,12,17)(H,13,14)(H,15,16)(H,18,19)/t5-,6-/m0/s1
InChIKey RWSXRVCMGQZWBV-WDSKDSINSA-N
PubChem Compound ID 124886
Drug Binding Sites of Target  Top
PDB ID: 3LEO      Structure of human Leukotriene C4 synthase mutant R31Q in complex with glutathione
Method X-ray diffraction Resolution 2.10 Å Mutation Yes [1]
PDB Sequence
HHHHHHKDEV
5
ALLAAVTLLG
15
VLLQAYFSLQ
25
VISARQAFRV
35
SPPLTTGPPE
45

FERVYRAQVN
55
CSEYFPLFLA
65
TLWVAGIFFH
75
EGAAALCGLV
85
YLFARLRYFQ
95

GYARSAQLRL
105
APLYASARAL
115
WLLVALAALG
125
LLAHFLPAAL
135
RAALLGRLRT
145
Residue
Distance (Å)
ARG51
2.803
ASN55
2.883
GLU58
2.742
TYR59
2.683
Residue
Distance (Å)
TYR93
2.731
TYR97
2.737
ARG104
2.898
LEU108
3.456
PDB ID: 3PCV      Crystal structure analysis of human leukotriene C4 synthase at 1.9 angstrom resolution
Method X-ray diffraction Resolution 1.90 Å Mutation No [2]
PDB Sequence
MKDEVALLAA
10
VTLLGVLLQA
20
YFSLQVISAR
30
RAFRVSPPLT
40
TGPPEFERVY
50

RAQVNCSEYF
60
PLFLATLWVA
70
GIFFHEGAAA
80
LCGLVYLFAR
90
LRYFQGYARS
100

AQLRLAPLYA
110
SARALWLLVA
120
LAALGLLAHF
130
LPAALRAALL
140
GRLRTL
Residue
Distance (Å)
ARG51
2.885
ASN55
2.952
GLU58
2.613
TYR59
2.616
Residue
Distance (Å)
TYR93
2.844
TYR97
2.692
ARG104
2.902
LEU108
3.403
PDB ID: 2UUH      Crystal structure of Human Leukotriene C4 Synthase in complex with substrate glutathione
Method X-ray diffraction Resolution 2.15 Å Mutation No [3]
PDB Sequence
HHHHHHKDEV
5
ALLAAVTLLG
15
VLLQAYFSLQ
25
VISARRAFRV
35
SPPLTTGPPE
45

FERVYRAQVN
55
CSEYFPLFLA
65
TLWVAGIFFH
75
EGAAALCGLV
85
YLFARLRYFQ
95

GYARSAQLRL
105
APLYASARAL
115
WLLVALAALG
125
LLAHFLPAAL
135
RAALLGRLRT
145

L
Residue
Distance (Å)
ARG51
2.671
ASN55
2.879
GLU58
2.506
TYR59
2.737
Residue
Distance (Å)
TYR93
2.758
TYR97
2.817
ARG104
2.874
LEU108
3.360
PDB ID: 5HV9      Human LTC4S mutant-S36E
Method X-ray diffraction Resolution 3.00 Å Mutation Yes [4]
PDB Sequence
VALLAAVTLL
14
GVLLQAYFSL
24
QVISARRAFR
34
VEPPLTTGPP
44
EFERVYRAQV
54

NCSEYFPLFL
64
ATLWVAGIFF
74
HEGAAALCGL
84
VYLFARLRYF
94
QGYARSAQLR
104

LAPLYASARA
114
LWLLVALAAL
124
GLLAHFLPAA
134
LRAALLGRLR
144
TLL
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Residue
Distance (Å)
ARG51
3.441
ASN55
3.033
GLU58
3.297
TYR59
3.019
Residue
Distance (Å)
TYR93
2.913
TYR97
2.333
ARG104
3.516
LEU108
3.372
PDB ID: 3B29      Human leukotriene C4 synthase in complex with dodecyl-beta-D-selenomaltoside
Method X-ray diffraction Resolution 3.20 Å Mutation No [5]
PDB Sequence
KDEVALLAAV
11
TLLGVLLQAY
21
FSLQVISARR
31
AFRVSPPLTT
41
GPPEFERVYR
51

AQVNCSEYFP
61
LFLATLWVAG
71
IFFHEGAAAL
81
CGLVYLFARL
91
RYFQGYARSA
101

QLRLAPLYAS
111
ARALWLLVAL
121
AALGLLAHFL
131
PAALRAALLG
141
RL
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Residue
Distance (Å)
ARG51
2.795
ASN55
2.622
GLU58
2.415
TYR59
3.041
Residue
Distance (Å)
TYR93
2.629
TYR97
2.962
ARG104
3.073
LEU108
3.361
PDB ID: 2PNO      Crystal structure of human leukotriene C4 synthase
Method X-ray diffraction Resolution 3.30 Å Mutation No [6]
PDB Sequence
KDEVALLAAV
11
TLLGVLLQAY
21
FSLQVISARR
31
AFRVSPPLTT
41
GPPEFERVYR
51

AQVNCSEYFP
61
LFLATLWVAG
71
IFFHEGAAAL
81
CGLVYLFARL
91
RYFQGYARSA
101

QLRLAPLYAS
111
ARALWLLVAL
121
AALGLLAHFL
131
PAALRAALLG
141
RLRTLL
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .GSH or .GSH2 or .GSH3 or :3GSH;style chemicals stick;color identity;select .A:51 or .A:55 or .A:58 or .A:59 or .A:93 or .A:97 or .A:104 or .A:108; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
ARG51
2.559
ASN55
2.749
GLU58
2.361
TYR59
2.785
Residue
Distance (Å)
TYR93
2.630
TYR97
2.876
ARG104
2.888
LEU108
3.327
References  Top
REF 1 Arginine 104 is a key catalytic residue in leukotriene C4 synthase. J Biol Chem. 2010 Dec 24;285(52):40771-6.
REF 2 The catalytic architecture of leukotriene C4 synthase with two arginine residues. J Biol Chem. 2011 May 6;286(18):16392-401.
REF 3 Structural basis for synthesis of inflammatory mediators by human leukotriene C4 synthase. Nature. 2007 Aug 2;448(7153):613-6.
REF 4 Phosphorylation of Leukotriene C4 Synthase at Serine 36 Impairs Catalytic Activity. J Biol Chem. 2016 Aug 26;291(35):18410-8.
REF 5 Seleno-detergent MAD phasing of leukotriene C4 synthase in complex with dodecyl--D-selenomaltoside. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2011 Dec 1;67(Pt 12):1666-73.
REF 6 Crystal structure of a human membrane protein involved in cysteinyl leukotriene biosynthesis. Nature. 2007 Aug 2;448(7153):609-12.

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