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4JA9

Rat PP5 apo

Functional Information from GO Data
ChainGOidnamespacecontents
A0001933biological_processnegative regulation of protein phosphorylation
A0001965molecular_functionG-protein alpha-subunit binding
A0003723molecular_functionRNA binding
A0004721molecular_functionphosphoprotein phosphatase activity
A0004722molecular_functionprotein serine/threonine phosphatase activity
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0008017molecular_functionmicrotubule binding
A0010288biological_processresponse to lead ion
A0016020cellular_componentmembrane
A0016787molecular_functionhydrolase activity
A0016791molecular_functionphosphatase activity
A0017018molecular_functionmyosin phosphatase activity
A0031072molecular_functionheat shock protein binding
A0032991cellular_componentprotein-containing complex
A0042802molecular_functionidentical protein binding
A0043025cellular_componentneuronal cell body
A0043066biological_processnegative regulation of apoptotic process
A0043204cellular_componentperikaryon
A0043278biological_processresponse to morphine
A0043531molecular_functionADP binding
A0044877molecular_functionprotein-containing complex binding
A0046872molecular_functionmetal ion binding
A0051879molecular_functionHsp90 protein binding
A0070262biological_processpeptidyl-serine dephosphorylation
A0070301biological_processcellular response to hydrogen peroxide
A0071276biological_processcellular response to cadmium ion
A0101031cellular_componentprotein folding chaperone complex
A1904550biological_processresponse to arachidonic acid
A1990635cellular_componentproximal dendrite
A2000324biological_processpositive regulation of glucocorticoid receptor signaling pathway
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 501
ChainResidue
AASP242
AHIS244
AASP271
AHIS427
AMG502
AHOH602

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE MG A 502
ChainResidue
AHIS352
AHIS427
AMG501
AHOH602
AASP242
AASP271
AASN303

Functional Information from PROSITE/UniProt
site_idPS00125
Number of Residues6
DetailsSER_THR_PHOSPHATASE Serine/threonine specific protein phosphatases signature. LRGNHE
ChainResidueDetails
ALEU300-GLU305

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton donor/acceptor => ECO:0000250|UniProtKB:P53041
ChainResidueDetails
AHIS304

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:26182372, ECO:0007744|PDB:4JA7
ChainResidueDetails
AASP242

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P53041
ChainResidueDetails
AHIS244
AARG275
AARG400
AHIS427

site_idSWS_FT_FI4
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:26182372, ECO:0007744|PDB:4JA7, ECO:0007744|PDB:4JA9
ChainResidueDetails
AASP271
AASN303
AHIS352

218853

PDB entries from 2024-04-24

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