Structure of PDB 2hv7 Chain E

Receptor sequence
>2hv7E (length=301) Species: 9606 (Homo sapiens) [Search protein sequence]
NFIIPKKEIHTVPDMGKWKRSQAYADYIGFILTLNEGVKGKKLTFEYRVS
EAIEKLVALLNTLDRWIDETPPVDQPSRFGNKAYRTWYAKLDEEAENLVA
TVVPTHLAAAVPEVAVYLKESVGNSTRIDYGTGHEAAFAAFLCCLCKIGV
LRVDDQIAIVFKVFNRYLEVMRKLQKTYRMEPAGSQGVWGLDDFQFLPFI
WGSSQLIDHPYLEPRHFVDEKAVNENHKDYMFLECILFITEMKTGPFAEH
SNQLWNISAVPSWSKVNQGLIRMYKAECLEKFPVIQHFKFGSLLPIHPVT
S
3D structure
PDB2hv7 Structure and mechanism of the phosphotyrosyl phosphatase activator.
ChainE
Resolution2.5 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 5.2.1.8: peptidylprolyl isomerase.
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 ADP E R148 G152 T153 A204 G205 S206 P304 V305 R127 G131 T132 A183 G184 S185 P283 V284
Gene Ontology
Molecular Function
GO:0003755 peptidyl-prolyl cis-trans isomerase activity
GO:0004721 phosphoprotein phosphatase activity
GO:0005102 signaling receptor binding
GO:0005515 protein binding
GO:0005524 ATP binding
GO:0008160 protein tyrosine phosphatase activator activity
GO:0019211 phosphatase activator activity
GO:0019888 protein phosphatase regulator activity
GO:0019902 phosphatase binding
GO:0042803 protein homodimerization activity
GO:0046872 metal ion binding
GO:0051721 protein phosphatase 2A binding
Biological Process
GO:0007052 mitotic spindle organization
GO:0043065 positive regulation of apoptotic process
Cellular Component
GO:0000159 protein phosphatase type 2A complex
GO:0005634 nucleus
GO:0005654 nucleoplasm
GO:0005737 cytoplasm
GO:0034704 calcium channel complex
GO:0070062 extracellular exosome
GO:1904949 ATPase complex

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Molecular Function
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Cellular Component
External links
PDB RCSB:2hv7, PDBe:2hv7, PDBj:2hv7
PDBsum2hv7
PubMed16916641
UniProtQ15257|PTPA_HUMAN Serine/threonine-protein phosphatase 2A activator (Gene Name=PTPA)

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