Binding Site Information of Target

Content Navigation (  All   None )                                      
Target General Information
Drug Binding Sites of Target
References
Target General Information  Top
Target ID T46642 Target Info
Target Name Arachidonate 5-lipoxygenase activating protein (FLAP)
Synonyms MK-886-binding protein; FLAP; ALOX5AP
Target Type Discontinued Target
Gene Name ALOX5AP
UniProt ID
AL5AP_HUMAN
Drug Binding Sites of Target  Top
Ligand Name: MK-591 Ligand Info
Structure Description Crystal structure of human FLAP with MK-591 PDB:2Q7M
Method X-ray diffraction Resolution 4.25 Å Mutation Yes [1]
PDB Sequence
MDQETVGNVV
10
LLAIVTLISV
20
VQNGFFAHKV
30
EHESRTQNGR
40
SFQRTGTLAF
50

ERVYTANQNC
60
VDAYPTFLAV
70
LWSAGLLCSQ
80
VPAAFAGLMY
90
LFVRQKYFVG
100

YLGERTQSTP
110
GYIFGKRIIL
120
FLFLMSVAGI
130
FNYYLIFFF
Residue
Distance (Å)
VAL20
4.503
VAL21
3.472
ASN23
3.310
GLY24
2.976
PHE25
2.881
ALA27
3.241
HIS28
3.652
ASN57
4.538
ASN59
4.362
VAL61
4.522
ASP62
3.235
Residue
Distance (Å)
ALA63
3.393
THR66
4.155
TYR90
4.428
TYR112
3.305
ILE113
3.355
PHE114
3.703
LYS116
2.747
ILE119
2.763
LEU120
3.338
PHE123
3.498
Ligand Name: DG031 Ligand Info
Structure Description Crystal Structures of FLAP bound to DG-031 PDB:6VGC
Method X-ray diffraction Resolution 2.37 Å Mutation No [2]
PDB Sequence
SLDQETVGNV
9
VLLAIVTLIS
19
VVQNGFFAHK
29
VEHESRTTGT
47
LAFERVYTAN
57

QNCVDAYPTF
67
LAVLWSAGLL
77
CSQVPAAFAG
87
LMYLFVRQKY
97
FVGYLPGYIF
114

GKRIILFLFL
124
MSVAGIFNYY
134
LIFFFGSDFE
144
NYIATISTTI
154
SPLL
Residue
Distance (Å)
ASN59
4.936
ASP62
3.498
ALA63
3.650
THR66
3.642
TYR112
3.407
Residue
Distance (Å)
ILE113
3.747
PHE114
4.133
LYS116
2.242
ILE119
3.544
LEU120
4.898
Ligand Name: MK-886 Ligand Info
Structure Description Crystal Structures of FLAP bound to MK-866 PDB:6VGI
Method X-ray diffraction Resolution 2.61 Å Mutation No [2]
PDB Sequence
SLDQETVGNV
9
VLLAIVTLIS
19
VVQNGFFAHK
29
VEHESRTGTL
48
AFERVYTANQ
58

NCVDAYPTFL
68
AVLWSAGLLC
78
SQVPAAFAGL
88
MYLFVRQKYF
98
VGYIFGKRII
119

LFLFLMSVAG
129
IFNYYLIFFF
139
GSDFENYIAT
149
ISTTISPLL
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .QY7 or .QY72 or .QY73 or :3QY7;style chemicals stick;color identity;select .A:20 or .A:21 or .A:23 or .A:24 or .A:25 or .A:27 or .A:28; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
VAL20
3.631
VAL21
3.837
ASN23
4.265
GLY24
3.227
Residue
Distance (Å)
PHE25
3.211
ALA27
3.904
HIS28
3.683
Ligand Name: 3-[3-(3,3-Dimethylbutanoyl)-1-(4-Iodobenzyl)-5-(Quinolin-2-Ylmethoxy)-1h-Indol-2-Yl]-2,2-Dimethylpropanoic Acid Ligand Info
Structure Description Crystal structure of human FLAP with an iodinated analog of MK-591 PDB:2Q7R
Method X-ray diffraction Resolution 4.00 Å Mutation Yes [1]
PDB Sequence
DQETVGNVVL
11
LAIVTLISVV
21
QNGFFAHKVE
31
HESRTQNGRS
41
FQRTGTLAFE
51

RVYTANQNCV
61
DAYPTFLAVL
71
WSAGLLCSQV
81
PAAFAGLYLF
92
VRQKYFVGYL
102

GERTQSTPGY
112
IFGKRIILFL
122
FLSVAGIFNY
133
YLIFFFG
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .3CS or .3CS2 or .3CS3 or :33CS;style chemicals stick;color identity;select .A:59 or .A:62 or .A:63 or .A:66 or .A:90 or .A:112 or .A:113 or .A:114 or .A:115 or .A:116 or .A:117 or .A:119 or .A:120 or .A:123; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
ASN59
4.655
ASP62
3.543
ALA63
3.851
THR66
3.886
TYR90
4.943
TYR112
3.909
ILE113
4.568
Residue
Distance (Å)
PHE114
4.127
GLY115
4.483
LYS116
2.983
ARG117
4.989
ILE119
2.956
LEU120
2.996
PHE123
3.557
Ligand Name: Selenomethionine Ligand Info
Structure Description Crystal structure of human FLAP with an iodinated analog of MK-591 PDB:2Q7R
Method X-ray diffraction Resolution 4.00 Å Mutation Yes [1]
PDB Sequence
DQETVGNVVL
11
LAIVTLISVV
21
QNGFFAHKVE
31
HESRTQNGRS
41
FQRTGTLAFE
51

RVYTANQNCV
61
DAYPTFLAVL
71
WSAGLLCSQV
81
PAAFAGLYLF
92
VRQKYFVGYL
102

GERTQSTPGY
112
IFGKRIILFL
122
FLSVAGIFNY
133
YLIFFFG
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .MSE or .MSE2 or .MSE3 or :3MSE;style chemicals stick;color identity;select .A:2 or .A:3 or .A:5 or .A:6 or .A:74 or .A:75 or .A:77 or .A:78 or .A:79 or .A:82 or .A:83 or .A:85 or .A:86 or .A:87 or .A:88 or .A:90 or .A:91 or .A:92 or .A:93 or .A:118 or .A:121 or .A:122 or .A:123 or .A:124 or .A:126 or .A:127 or .A:128 or .A:129; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
ASP2
1.334
GLN3
3.348
THR5
3.584
VAL6
3.427
ALA74
2.870
GLY75
4.015
LEU77
4.619
CYS78
3.047
SER79
3.823
PRO82
3.870
ALA83
3.087
PHE85
2.762
ALA86
2.839
GLY87
3.292
Residue
Distance (Å)
LEU88
1.326
TYR90
1.328
LEU91
3.230
PHE92
2.849
VAL93
2.885
ILE118
3.299
PHE121
2.914
LEU122
3.419
PHE123
3.278
LEU124
1.329
SER126
1.331
VAL127
3.575
ALA128
2.933
GLY129
3.338
References  Top
REF 1 Crystal structure of inhibitor-bound human 5-lipoxygenase-activating protein. Science. 2007 Jul 27;317(5837):510-2.
REF 2 Structure-based, multi-targeted drug discovery approach to eicosanoid inhibition: Dual inhibitors of mPGES-1 and 5-lipoxygenase activating protein (FLAP). Biochim Biophys Acta Gen Subj. 2021 Feb;1865(2):129800.

If You Find Any Error in Data or Bug in Web Service, Please Kindly Report It to Dr. Zhou and Dr. Zhang.