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 Palmitoleic acid Ligand Info
Canonical SMILES CCCCCCC=CCCCCCCCC(=O)O
InChI 1S/C16H30O2/c1-2-3-4-5-6-7-8-9-10-11-12-13-14-15-16(17)18/h7-8H,2-6,9-15H2,1H3,(H,17,18)/b8-7-
InChIKey SECPZKHBENQXJG-FPLPWBNLSA-N
PubChem Compound ID 445638
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)
HIS1
4.085
GLU4
3.286
VAL5
4.173
LEU7
3.914
ALA10
3.516
VAL11
3.772
LEU14
3.911
LEU64
4.552
ALA65
4.176
Residue
Distance (Å)
TRP68
3.887
GLY71
4.569
ILE72
3.509
HIS75
4.288
GLY77
3.918
ALA78
4.033
ALA80
4.119
LEU81
3.783
LEU84
3.688
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 [2]
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)
HIS1
3.881
GLU4
3.401
VAL5
4.230
LEU64
4.550
Residue
Distance (Å)
ALA65
4.062
TRP68
3.884
GLY71
4.957
ILE72
3.311
PDB ID: 4JRZ      Human LTC4 synthase in complex with product analogs - implications for enzyme catalysis
Method X-ray diffraction Resolution 2.40 Å Mutation No [3]
PDB Sequence
MHHHHHHKDE
4
VALLAAVTLL
14
GVLLQAYFSL
24
QVISARRAFR
34
VSPPLTTGPP
44

EFERVYRAQV
54
NCSEYFPLFL
64
ATLWVAGIFF
74
HEGAAALCGL
84
VYLFARLRYF
94

QGYARSAQLR
104
LAPLYASARA
114
LFLLVALAAL
124
GLLAHFLPAA
134
LRAALLGRLR
144

TLLPWA
Residue
Distance (Å)
HIS1
3.571
GLU4
2.976
VAL5
3.943
Residue
Distance (Å)
ALA65
4.463
TRP68
3.947
ILE72
3.516
PDB ID: 4JC7      Human LTC4 synthase in complex with product analogs - implications for enzyme catalysis
Method X-ray diffraction Resolution 2.70 Å Mutation Yes [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
ALLVALAALG
125
LLAHFLPAAL
135
RAALLGRLRT
145

LLPWA
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Residue
Distance (Å)
HIS1
4.058
GLU4
3.239
VAL5
4.712
LEU64
4.879
Residue
Distance (Å)
ALA65
4.126
TRP68
3.892
GLY71
4.658
ILE72
3.483
PDB ID: 4JCZ      Human LTC4 synthase in complex with product analogs - implications for enzyme catalysis
Method X-ray diffraction Resolution 2.75 Å Mutation No [3]
PDB Sequence
HHKDEVALLA
9
AVTLLGVLLQ
19
AYFSLQVISA
29
RRAFRVSPPL
39
TTGPPEFERV
49

YRAQVNCSEY
59
FPLFLATLWV
69
AGIFFHEGAA
79
ALCGLVYLFA
89
RLRYFQGYAR
99

SAQLRLAPLY
109
ASARALWLLV
119
ALAALGLLAH
129
FLPAALRAAL
139
LGRLRTL
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set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .PAM or .PAM2 or .PAM3 or :3PAM;style chemicals stick;color identity;select .A:1 or .A:4 or .A:5 or .A:64 or .A:65 or .A:68 or .A:72; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
HIS1
3.758
GLU4
3.291
VAL5
4.653
LEU64
4.649
Residue
Distance (Å)
ALA65
4.154
TRP68
4.048
ILE72
3.499
PDB ID: 3HKK      Structure of human Leukotriene C4 synthase in complex with glutathione sulfonate
Method X-ray diffraction Resolution 2.90 Å Mutation No [4]
PDB Sequence
HKDEVALLAA
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
GRLRT
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set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .PAM or .PAM2 or .PAM3 or :3PAM;style chemicals stick;color identity;select .A:4 or .A:5 or .A:64 or .A:65 or .A:68 or .A:72; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
GLU4
3.214
VAL5
4.776
LEU64
4.747
Residue
Distance (Å)
ALA65
4.283
TRP68
3.812
ILE72
3.465
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 Structural basis for synthesis of inflammatory mediators by human leukotriene C4 synthase. Nature. 2007 Aug 2;448(7153):613-6.
REF 3 Crystal structures of leukotriene C4 synthase in complex with product analogs: implications for the enzyme mechanism. J Biol Chem. 2014 Feb 21;289(8):5199-207.
REF 4 Pre-steady state kinetics of human Leukotriene C4 synthase

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