Structure of PDB 3pfq Chain A Binding Site BS05
Receptor Information
>3pfq Chain A (length=523) Species:
10116
(Rattus norvegicus) [
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KHKFKIHTYSSPTFCDHCGSLLYGLIHQGMKCDTCMMNVHKRCVMNVPSL
CGTDHTERRGRIYIQAHIDREVLIVVVRDAKNLVPMDPNGLSDPYVKLKL
IPDPKSESKQKTKTIKSSLNPEWNETFRFQLKESDKDRRLSVEIWDWDLT
SRNDFMGSLSFGISELQKAGVDGWFKLLSQEEGEYFNVPVPPLTDFNFLM
VLGKGSFGKVMLSERKGTDELYAVKILKKDVVIQDDDVECTMVEKRVLAL
PGKPPFLTQLHSCFQTMDRLYFVMEYVNGGDLMYHIQQVGRFKEPHAVFY
AAEIAIGLFFLQSKGIIYRDLKLDNVMLDSEGHIKIADFGMCKENIWDGV
TTKTFCGTPDYIAPEIIAYQPYGKSVDWWAFGVLLYEMLAGQAPFEGEDE
DELFQSIMEHNVAYPKSMSKEAVAICKGLMTKHPGKRLGCGPEGERDIKE
HAFFRYIDWEKLERKEIQPPYKPKASGRNAENFDRFFTRHPPVLTPPDQE
VIRNIDQSEFEGFSFVNSEFLKP
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
3pfq Chain A Residue 751 [
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Receptor-Ligand Complex Structure
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PDB
3pfq
Crystal Structure and Allosteric Activation of Protein Kinase C beta II
Resolution
4.0 Å
Binding residue
(original residue number in PDB)
H140 C143
Binding residue
(residue number reindexed from 1)
H40 C43
Annotation score
1
Enzymatic activity
Catalytic site (original residue number in PDB)
D466 K468 D470 N471 D484 T504
Catalytic site (residue number reindexed from 1)
D320 K322 D324 N325 D338 T358
Enzyme Commision number
2.7.11.13
: protein kinase C.
Gene Ontology
Molecular Function
GO:0003682
chromatin binding
GO:0004672
protein kinase activity
GO:0004674
protein serine/threonine kinase activity
GO:0004697
diacylglycerol-dependent serine/threonine kinase activity
GO:0004698
calcium,diacylglycerol-dependent serine/threonine kinase activity
GO:0005080
protein kinase C binding
GO:0005246
calcium channel regulator activity
GO:0005515
protein binding
GO:0005524
ATP binding
GO:0008270
zinc ion binding
GO:0030374
nuclear receptor coactivator activity
GO:0035403
histone H3T6 kinase activity
GO:0042393
histone binding
GO:0046872
metal ion binding
GO:0050681
nuclear androgen receptor binding
GO:0106310
protein serine kinase activity
Biological Process
GO:0002250
adaptive immune response
GO:0006325
chromatin organization
GO:0006338
chromatin remodeling
GO:0006357
regulation of transcription by RNA polymerase II
GO:0006468
protein phosphorylation
GO:0006816
calcium ion transport
GO:0006874
intracellular calcium ion homeostasis
GO:0006915
apoptotic process
GO:0007207
phospholipase C-activating G protein-coupled acetylcholine receptor signaling pathway
GO:0009410
response to xenobiotic stimulus
GO:0009749
response to glucose
GO:0010827
regulation of D-glucose transmembrane transport
GO:0010829
negative regulation of D-glucose transmembrane transport
GO:0014059
regulation of dopamine secretion
GO:0016310
phosphorylation
GO:0018894
dibenzo-p-dioxin metabolic process
GO:0030949
positive regulation of vascular endothelial growth factor receptor signaling pathway
GO:0032024
positive regulation of insulin secretion
GO:0033280
response to vitamin D
GO:0035556
intracellular signal transduction
GO:0040008
regulation of growth
GO:0042113
B cell activation
GO:0042488
positive regulation of odontogenesis of dentin-containing tooth
GO:0043123
positive regulation of canonical NF-kappaB signal transduction
GO:0043687
post-translational protein modification
GO:0045471
response to ethanol
GO:0045766
positive regulation of angiogenesis
GO:0045893
positive regulation of DNA-templated transcription
GO:0046627
negative regulation of insulin receptor signaling pathway
GO:0050853
B cell receptor signaling pathway
GO:0050861
positive regulation of B cell receptor signaling pathway
GO:0071322
cellular response to carbohydrate stimulus
GO:0099171
presynaptic modulation of chemical synaptic transmission
GO:2000300
regulation of synaptic vesicle exocytosis
Cellular Component
GO:0005634
nucleus
GO:0005654
nucleoplasm
GO:0005737
cytoplasm
GO:0005813
centrosome
GO:0005829
cytosol
GO:0005886
plasma membrane
GO:0008091
spectrin
GO:0016020
membrane
GO:0031526
brush border membrane
GO:0044305
calyx of Held
GO:0099523
presynaptic cytosol
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Molecular Function
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Biological Process
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Cellular Component
External links
PDB
RCSB:3pfq
,
PDBe:3pfq
,
PDBj:3pfq
PDBsum
3pfq
PubMed
21215369
UniProt
P68403
|KPCB_RAT Protein kinase C beta type (Gene Name=Prkcb)
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