Structure of PDB 3hvq Chain A
Receptor sequence
>3hvqA (length=294) Species:
9606
(Homo sapiens) [
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LNLDSIIGRLLEVQGSRPGKNVQLTENEIRGLCLKSREIFLSQPILLELE
APLKICGDIHGQYYDLLRLFEYGGFPPESNYLFLGDYVDRGKQSLETICL
LLAYKIKYPENFFLLRGNHECASINRIYGFYDECKRRYNIKLWKTFTDCF
NCLPIAAIVDEKIFCCHGGLSPDLQSMEQIRRIMRPTDVPDQGLLCDLLW
SDPDKDVQGWGENDRGVSFTFGAEVVAKFLHKHDLDLICRAHQVVEDGYE
FFAKRQLVTLFSAPNYCGEFDNAGAMMSVDETLMCSFQILKPAD
3D structure
PDB
3hvq
Spinophilin directs protein phosphatase 1 specificity by blocking substrate binding sites.
Chain
A
Resolution
2.2 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB)
D64 H66 D92 D95 R96 N124 H125 H173 R221 H248
Catalytic site (residue number reindexed from 1)
D58 H60 D86 D89 R90 N118 H119 H167 R215 H242
Enzyme Commision number
3.1.3.16
: protein-serine/threonine phosphatase.
Interaction with ligand
Site
#
Ligand
Ligand
chain
Binding residues on receptor
(original residue number in PDB)
Binding residues on receptor
(residue number reindexed from 1)
Binding affinity
BS01
MN
A
D64 H66 D92
D58 H60 D86
BS02
MN
A
D92 N124 H173 H248
D86 N118 H167 H242
Gene Ontology
Molecular Function
GO:0004721
phosphoprotein phosphatase activity
GO:0004722
protein serine/threonine phosphatase activity
GO:0005506
iron ion binding
GO:0005515
protein binding
GO:0008157
protein phosphatase 1 binding
GO:0016787
hydrolase activity
GO:0016791
phosphatase activity
GO:0017018
myosin phosphatase activity
GO:0043021
ribonucleoprotein complex binding
GO:0044877
protein-containing complex binding
GO:0046872
metal ion binding
GO:0046914
transition metal ion binding
GO:0098641
cadherin binding involved in cell-cell adhesion
Biological Process
GO:0005977
glycogen metabolic process
GO:0005979
regulation of glycogen biosynthetic process
GO:0005981
regulation of glycogen catabolic process
GO:0006470
protein dephosphorylation
GO:0010288
response to lead ion
GO:0016311
dephosphorylation
GO:0030324
lung development
GO:0032922
circadian regulation of gene expression
GO:0042752
regulation of circadian rhythm
GO:0043153
entrainment of circadian clock by photoperiod
GO:0043247
telomere maintenance in response to DNA damage
GO:0043558
regulation of translational initiation in response to stress
GO:0045725
positive regulation of glycogen biosynthetic process
GO:0048754
branching morphogenesis of an epithelial tube
GO:0051301
cell division
GO:0060828
regulation of canonical Wnt signaling pathway
GO:0098609
cell-cell adhesion
GO:2001241
positive regulation of extrinsic apoptotic signaling pathway in absence of ligand
Cellular Component
GO:0000164
protein phosphatase type 1 complex
GO:0000781
chromosome, telomeric region
GO:0005634
nucleus
GO:0005654
nucleoplasm
GO:0005730
nucleolus
GO:0005737
cytoplasm
GO:0005829
cytosol
GO:0005886
plasma membrane
GO:0005912
adherens junction
GO:0042587
glycogen granule
GO:0043025
neuronal cell body
GO:0043197
dendritic spine
GO:0043204
perikaryon
GO:0070062
extracellular exosome
GO:0072357
PTW/PP1 phosphatase complex
GO:0098793
presynapse
GO:0098794
postsynapse
GO:0098978
glutamatergic synapse
View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB
RCSB:3hvq
,
PDBe:3hvq
,
PDBj:3hvq
PDBsum
3hvq
PubMed
20305656
UniProt
P62136
|PP1A_HUMAN Serine/threonine-protein phosphatase PP1-alpha catalytic subunit (Gene Name=PPP1CA)
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