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 T56510 Target Info
Target Name Apoptosis regulator Bcl-xL (BCL-xL)
Synonyms Bcl2like protein 1; Bcl2L1; Bcl2-L-1; Bcl-XL; Bcl-2-like protein 1; BCLX; BCL2L; Apoptosis regulator Bcl-X
Target Type Clinical trial Target
Gene Name BCL2L1
Biochemical Class B-cell lymphoma Bcl-2
UniProt ID
B2CL1_HUMAN
Ligand General Information  Top
Ligand Name Venetoclax Ligand Info
Canonical SMILES CC1(CCC(=C(C1)C2=CC=C(C=C2)Cl)CN3CCN(CC3)C4=CC(=C(C=C4)C(=O)NS(=O)(=O)C5=CC(=C(C=C5)NCC6CCOCC6)[N+](=O)[O-])OC7=CN=C8C(=C7)C=CN8)C
InChI 1S/C45H50ClN7O7S/c1-45(2)15-11-33(39(26-45)31-3-5-34(46)6-4-31)29-51-17-19-52(20-18-51)35-7-9-38(42(24-35)60-36-23-32-12-16-47-43(32)49-28-36)44(54)50-61(57,58)37-8-10-40(41(25-37)53(55)56)48-27-30-13-21-59-22-14-30/h3-10,12,16,23-25,28,30,48H,11,13-15,17-22,26-27,29H2,1-2H3,(H,47,49)(H,50,54)
InChIKey LQBVNQSMGBZMKD-UHFFFAOYSA-N
PubChem Compound ID 49846579
Drug Binding Sites of Target  Top
PDB ID: 6O0K      crystal structure of BCL-2 with venetoclax
Method X-ray diffraction Resolution 1.62 Å Mutation No [1]
PDB Sequence
YDNREIVMKY
18
IHYKLSQRGY
28
EWDAGDDSEV
92
VHLTLRQAGD
102
DFSRRYRRDF
112

AEMSSQLHLT
122
PFTARGRFAT
132
VVEELFRDGV
142
NWGRIVAFFE
152
FGGVMCVESV
162

NREMSPLVDN
172
IALWMTEYLN
182
RHLHTWIQDN
192
GGWDAFVELY
202
G
Residue
Distance (Å)
GLN99
4.770
ALA100
3.123
ASP103
2.772
PHE104
3.735
ARG107
3.306
TYR108
3.688
ASP111
3.665
PHE112
3.777
MET115
3.612
VAL133
4.143
GLU136
3.833
LEU137
3.658
Residue
Distance (Å)
ASN143
3.546
TRP144
3.292
GLY145
2.960
ARG146
3.839
VAL148
3.383
ALA149
3.511
GLU152
3.684
PHE153
3.630
VAL156
3.860
PHE198
3.529
TYR202
3.448
PDB ID: 6O0M      crystal structure of BCL-2 F104L mutation with venetoclax
Method X-ray diffraction Resolution 1.75 Å Mutation Yes [1]
PDB Sequence
GYDNREIVMK
17
YIHYKLSQRG
27
YEWDAGDSEV
92
VHLTLRQAGD
102
DLSRRYRRDF
112

AEMSSQLHLT
122
PFTARGRFAT
132
VVEELFRDGV
142
NWGRIVAFFE
152
FGGVMCVESV
162

NREMSPLVDN
172
IALWMTEYLN
182
RHLHTWIQDN
192
GGWDAFVELY
202
G
Residue
Distance (Å)
GLN99
4.916
ALA100
3.134
GLY101
4.995
ASP103
2.783
LEU104
3.520
ARG107
3.321
TYR108
3.818
ASP111
3.998
PHE112
3.394
MET115
3.656
VAL133
4.243
GLU136
3.793
Residue
Distance (Å)
LEU137
3.706
ASN143
3.682
TRP144
3.360
GLY145
3.021
ARG146
3.973
VAL148
3.297
ALA149
3.632
GLU152
3.548
PHE153
3.500
VAL156
3.558
PHE198
3.441
TYR202
3.420
PDB ID: 6O0P      crystal structure of BCL-2 G101A mutation with venetoclax
Method X-ray diffraction Resolution 1.80 Å Mutation Yes [1]
PDB Sequence
YDNREIVMKY
18
IHYKLSQRGY
28
EWDAGDDSEV
92
VHLTLRQAAD
102
DFSRRYRRDF
112

AEMSSQLHLT
122
PFTARGRFAT
132
VVEELFRDGV
142
NWGRIVAFFE
152
FGGVMCVESV
162

NREMSPLVDN
172
IALWMTEYLN
182
RHLHTWIQDN
192
GGWDAFVELY
202
G
Residue
Distance (Å)
GLN99
4.427
ALA100
3.123
ASP103
2.946
PHE104
3.691
ARG107
3.385
TYR108
3.521
ASP111
3.665
PHE112
3.993
GLU114
4.436
MET115
3.699
VAL133
4.364
GLU136
3.806
Residue
Distance (Å)
LEU137
3.634
ASN143
3.673
TRP144
3.371
GLY145
3.017
ARG146
4.048
VAL148
3.345
ALA149
3.511
GLU152
3.695
PHE153
3.699
VAL156
3.748
PHE198
3.444
TYR202
3.485
PDB ID: 6O0L      crystal structure of BCL-2 G101V mutation with venetoclax
Method X-ray diffraction Resolution 2.20 Å Mutation Yes [1]
PDB Sequence
YDNREIVMKY
18
IHYKLSQRGY
28
EWDAGSEVVH
94
LTLRQAVDDF
104
SRRYRRDFAE
114

MSSQLHLTPF
124
TARGRFATVV
134
EELFRDGVNW
144
GRIVAFFEFG
154
GVMCVESVNR
164

EMSPLVDNIA
174
LWMTEYLNRH
184
LHTWIQDNGG
194
WDAFVELYG
Click to Show 3D Structure of This Binding Site
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Residue
Distance (Å)
GLN99
4.788
ALA100
3.166
ASP103
2.814
PHE104
3.788
ARG107
3.374
TYR108
3.350
ASP111
3.795
PHE112
3.990
MET115
3.705
VAL133
3.918
GLU136
3.825
LEU137
3.519
Residue
Distance (Å)
ASN143
3.810
TRP144
3.394
GLY145
2.968
ARG146
3.957
VAL148
3.390
ALA149
3.673
GLU152
3.347
PHE153
3.666
VAL156
3.419
PHE198
3.265
TYR202
3.334
References  Top
REF 1 Structures of BCL-2 in complex with venetoclax reveal the molecular basis of resistance mutations. Nat Commun. 2019 Jun 3;10(1):2385.

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