Structure of PDB 1phk Chain A Binding Site BS01
Receptor Information
>1phk Chain A (length=277) Species:
9986
(Oryctolagus cuniculus) [
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FYENYEPKEILGRGVSSVVRRCIHKPTCKEYAVKIIDVTGGGSFSAEEVQ
ELREATLKEVDILRKVSGHPNIIQLKDTYETNTFFFLVFDLMKKGELFDY
LTEKVTLSEKETRKIMRALLEVICALHKLNIVHRDLKPENILLDDDMNIK
LTDFGFSCQLDPGEKLREVCGTPSYLAPEIIECSMNDNHPGYGKEVDMWS
TGVIMYTLLAGSPPFWHRKQMLMLRMIMSGNYQFGSPEWDDYSDTVKDLV
SRFLVVQPQKRYTAEEALAHPFFQQYV
Ligand information
Ligand ID
MN
InChI
InChI=1S/Mn/q+2
InChIKey
WAEMQWOKJMHJLA-UHFFFAOYSA-N
SMILES
Software
SMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0
[Mn+2]
CACTVS 3.341
[Mn++]
Formula
Mn
Name
MANGANESE (II) ION
ChEMBL
DrugBank
DB06757
ZINC
PDB chain
1phk Chain A Residue 383 [
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Receptor-Ligand Complex Structure
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PDB
1phk
Two structures of the catalytic domain of phosphorylase kinase: an active protein kinase complexed with substrate analogue and product.
Resolution
2.2 Å
Binding residue
(original residue number in PDB)
N154 D167
Binding residue
(residue number reindexed from 1)
N140 D153
Annotation score
1
Enzymatic activity
Catalytic site (original residue number in PDB)
D149 K151 N154 D167 T186
Catalytic site (residue number reindexed from 1)
D135 K137 N140 D153 T172
Enzyme Commision number
2.7.11.1
: non-specific serine/threonine protein kinase.
2.7.11.19
: phosphorylase kinase.
2.7.11.26
: [tau protein] kinase.
Gene Ontology
Molecular Function
GO:0004672
protein kinase activity
GO:0004689
phosphorylase kinase activity
GO:0005516
calmodulin binding
GO:0005524
ATP binding
Biological Process
GO:0005977
glycogen metabolic process
GO:0006468
protein phosphorylation
Cellular Component
GO:0005964
phosphorylase kinase complex
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Molecular Function
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Cellular Component
External links
PDB
RCSB:1phk
,
PDBe:1phk
,
PDBj:1phk
PDBsum
1phk
PubMed
7663944
UniProt
P00518
|PHKG1_RABIT Phosphorylase b kinase gamma catalytic chain, skeletal muscle/heart isoform (Gene Name=PHKG1)
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