Structure of PDB 5fwg Chain B Binding Site BS01
Receptor Information
>5fwg Chain B (length=217) Species:
10116
(Rattus norvegicus) [
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PMILGYWNVRGLTHPIRLLLEYTDSSYEEKRYAMGDAPDYDRSQWLNEKF
KLGLDFPNLPYLIDGSRKITQSNAIMRYLARKHHLCGETEEERIRADIVE
NQVMDNRMQLIMLCYNPDFEKQKPEFLKTIPEKMKLYSEFLGKRPWFAGD
KVTYVDFLAYDILDQYHIFEPKCLDAFPNLKDFLARFEGLKKISAYMKSS
RYLSTPIFSKLAQWSNK
Ligand information
Ligand ID
GPR
InChI
InChI=1S/C24H27N3O7S/c25-17(24(33)34)9-10-19(28)27-18(23(32)26-11-20(29)30)12-35-22-16-8-4-2-6-14(16)13-5-1-3-7-15(13)21(22)31/h1-8,17-18,21-22,31H,9-12,25H2,(H,26,32)(H,27,28)(H,29,30)(H,33,34)/t17-,18-,21+,22+/m0/s1
InChIKey
JNNIZILNBMPOAC-MOXQZVSFSA-N
SMILES
Software
SMILES
OpenEye OEToolkits 1.5.0
c1ccc2c(c1)-c3ccccc3C(C2O)SCC(C(=O)NCC(=O)O)NC(=O)CCC(C(=O)O)N
OpenEye OEToolkits 1.5.0
c1ccc2c(c1)-c3ccccc3[C@H]([C@@H]2O)SC[C@@H](C(=O)NCC(=O)O)NC(=O)CC[C@@H](C(=O)O)N
CACTVS 3.341
N[C@@H](CCC(=O)N[C@@H](CS[C@H]1[C@H](O)c2ccccc2c3ccccc13)C(=O)NCC(O)=O)C(O)=O
ACDLabs 10.04
O=C(O)C(N)CCC(=O)NC(C(=O)NCC(=O)O)CSC3c1ccccc1c2c(cccc2)C3O
CACTVS 3.341
N[CH](CCC(=O)N[CH](CS[CH]1[CH](O)c2ccccc2c3ccccc13)C(=O)NCC(O)=O)C(O)=O
Formula
C24 H27 N3 O7 S
Name
(9R,10R)-9-(S-GLUTATHIONYL)-10-HYDROXY-9,10-DIHYDROPHENANTHRENE
ChEMBL
DrugBank
DB01834
ZINC
ZINC000015685338
PDB chain
5fwg Chain B Residue 218 [
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Receptor-Ligand Complex Structure
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PDB
5fwg
Enzymes harboring unnatural amino acids: mechanistic and structural analysis of the enhanced catalytic activity of a glutathione transferase containing 5-fluorotryptophan.
Resolution
2.0 Å
Binding residue
(original residue number in PDB)
Y6 X7 G11 L12 R42 X45 K49 N58 L59 Q71 S72 I111
Binding residue
(residue number reindexed from 1)
Y6 X7 G11 L12 R42 X45 K49 N58 L59 Q71 S72 I111
Annotation score
2
Binding affinity
PDBbind-CN
: -logKd/Ki=6.72,Kd=0.19uM
Enzymatic activity
Catalytic site (original residue number in PDB)
Y6 L12 R17
Catalytic site (residue number reindexed from 1)
Y6 L12 R17
Enzyme Commision number
2.5.1.18
: glutathione transferase.
Gene Ontology
Molecular Function
GO:0004364
glutathione transferase activity
GO:0005496
steroid binding
GO:0016151
nickel cation binding
GO:0016740
transferase activity
GO:0019899
enzyme binding
GO:0019901
protein kinase binding
GO:0042802
identical protein binding
GO:0042803
protein homodimerization activity
GO:0043295
glutathione binding
Biological Process
GO:0006629
lipid metabolic process
GO:0006693
prostaglandin metabolic process
GO:0006749
glutathione metabolic process
GO:0007608
sensory perception of smell
GO:0009410
response to xenobiotic stimulus
GO:0010038
response to metal ion
GO:0010288
response to lead ion
GO:0018916
nitrobenzene metabolic process
GO:0042178
xenobiotic catabolic process
GO:0043200
response to amino acid
GO:0045471
response to ethanol
GO:0048678
response to axon injury
GO:0051122
hepoxilin biosynthetic process
GO:0070458
cellular detoxification of nitrogen compound
GO:0071466
cellular response to xenobiotic stimulus
GO:1901687
glutathione derivative biosynthetic process
Cellular Component
GO:0005576
extracellular region
GO:0005737
cytoplasm
GO:0005829
cytosol
GO:0032991
protein-containing complex
View graph for
Molecular Function
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Biological Process
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Cellular Component
External links
PDB
RCSB:5fwg
,
PDBe:5fwg
,
PDBj:5fwg
PDBsum
5fwg
PubMed
9572843
UniProt
P04905
|GSTM1_RAT Glutathione S-transferase Mu 1 (Gene Name=Gstm1)
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