Structure of PDB 1tn8 Chain B Binding Site BS01
Receptor Information
>1tn8 Chain B (length=407) Species:
10116
(Rattus norvegicus) [
Search protein sequence
] [
Download receptor structure
] [
Download structure with residue number starting from 1
] [
View receptor structure
]
PVWSEPLYSLRPEHARERLQDDSVETVTSIEQAKVEEKIQEVFSSYKFNH
LVPRLVLQREKHFHYLKRGLRQLTDAYECLDASRPWLCYWILHSLELLDE
PIPQIVATDVCQFLELCQSPDGGFGGGPGQYPHLAPTYAAVNALCIIGTE
EAYNVINREKLLQYLYSLKQPDGSFLMHVGGEVDVRSAYCAASVASLTNI
ITPDLFEGTAEWIARCQNWEGGIGGVPGMEAHGGYTFCGLAALVILKKER
SLNLKSLLQWVTSRQMRFEGGFQGRCNKLVDGCYSFWQAGLLPLLHRALH
AQGDPALSMSHWMFHQQALQEYILMCCQCPAGGLLDKPGKSRDFYHTCYC
LSGLSIAQHFGSGAMLHDVVMGVPENVLQPTHPVYNIGPDKVIQATTHFL
QKPVPGF
Ligand information
>1tn8 Chain C (length=5) [
Search peptide sequence
] [
Download ligand structure
] [
Download structure with residue number starting from 1
] [
View ligand structure
]
GCVLS
Receptor-Ligand Complex Structure
Global view
Local view
Structure summary
[
Spin on
] [
Spin off
] [
Reset
]
[
High quality
] [
Low quality
]
[
White background
] [
Black background
]
[
Spin on
] [
Spin off
] [
Reset
]
[
High quality
] [
Low quality
]
[
White background
] [
Black background
]
PDB
1tn8
Crystallographic analysis of CaaX prenyltransferases complexed with substrates defines rules of protein substrate selectivity.
Resolution
2.25 Å
Binding residue
(original residue number in PDB)
W602 R702 Y861 H862
Binding residue
(residue number reindexed from 1)
W86 R186 Y345 H346
Enzymatic activity
Catalytic site (original residue number in PDB)
H748 R791 K794 D797 C799 Y800 D852 D859 H862
Catalytic site (residue number reindexed from 1)
H232 R275 K278 D281 C283 Y284 D336 D343 H346
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
View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB
RCSB:1tn8
,
PDBe:1tn8
,
PDBj:1tn8
PDBsum
1tn8
PubMed
15451670
UniProt
Q02293
|FNTB_RAT Protein farnesyltransferase subunit beta (Gene Name=Fntb)
[
Back to BioLiP
]