Structure of PDB 1nl4 Chain B Binding Site BS01
Receptor Information
>1nl4 Chain B (length=401) Species:
10116
(Rattus norvegicus) [
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LYSLRPEHARERLQDDSVETVTSIEQAKVEEKIQEVFSSYKFNHLVPRLV
LQREKHFHYLKRGLRQLTDAYECLDASRPWLCYWILHSLELLDEPIPQIV
ATDVCQFLELCQSPDGGFGGGPGQYPHLAPTYAAVNALCIIGTEEAYNVI
NREKLLQYLYSLKQPDGSFLMHVGGEVDVRSAYCAASVASLTNIITPDLF
EGTAEWIARCQNWEGGIGGVPGMEAHGGYTFCGLAALVILKKERSLNLKS
LLQWVTSRQMRFEGGFQGRCNKLVDGCYSFWQAGLLPLLHRALHAQGDPA
LSMSHWMFHQQALQEYILMCCQCPAGGLLDKPGKSRDFYHTCYCLSGLSI
AQHFGSGAMLHDVVMGVPENVLQPTHPVYNIGPDKVIQATTHFLQKPVPG
F
Ligand information
Ligand ID
ZN
InChI
InChI=1S/Zn/q+2
InChIKey
PTFCDOFLOPIGGS-UHFFFAOYSA-N
SMILES
Software
SMILES
CACTVS 3.341
[Zn++]
ACDLabs 10.04
OpenEye OEToolkits 1.5.0
[Zn+2]
Formula
Zn
Name
ZINC ION
ChEMBL
CHEMBL1236970
DrugBank
DB14532
ZINC
PDB chain
1nl4 Chain B Residue 500 [
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Receptor-Ligand Complex Structure
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PDB
1nl4
Novel and Selective Imidazole-containing Biphenyl Inhibitors of Protein Farnesyltransferase
Resolution
2.7 Å
Binding residue
(original residue number in PDB)
D297 C299 H362
Binding residue
(residue number reindexed from 1)
D275 C277 H340
Annotation score
1
Enzymatic activity
Catalytic site (original residue number in PDB)
H248 R291 K294 D297 C299 Y300 D352 D359 H362
Catalytic site (residue number reindexed from 1)
H226 R269 K272 D275 C277 Y278 D330 D337 H340
Enzyme Commision number
2.5.1.58
: protein farnesyltransferase.
Gene Ontology
Molecular Function
GO:0003824
catalytic activity
GO:0004311
farnesyltranstransferase activity
GO:0004659
prenyltransferase activity
GO:0004660
protein farnesyltransferase activity
GO:0005515
protein binding
GO:0008270
zinc ion binding
GO:0008318
protein prenyltransferase activity
GO:0042277
peptide binding
GO:0046872
metal ion binding
Biological Process
GO:0006629
lipid metabolic process
GO:0008283
cell population proliferation
GO:0008284
positive regulation of cell population proliferation
GO:0008285
negative regulation of cell population proliferation
GO:0014070
response to organic cyclic compound
GO:0018343
protein farnesylation
GO:0034097
response to cytokine
GO:0042060
wound healing
GO:0045787
positive regulation of cell cycle
GO:0048144
fibroblast proliferation
GO:0048145
regulation of fibroblast proliferation
GO:0048146
positive regulation of fibroblast proliferation
GO:0051770
positive regulation of nitric-oxide synthase biosynthetic process
Cellular Component
GO:0005875
microtubule associated complex
GO:0005965
protein farnesyltransferase complex
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Molecular Function
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Biological Process
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Cellular Component
External links
PDB
RCSB:1nl4
,
PDBe:1nl4
,
PDBj:1nl4
PDBsum
1nl4
PubMed
12657284
UniProt
Q02293
|FNTB_RAT Protein farnesyltransferase subunit beta (Gene Name=Fntb)
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