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1WAO

PP5 structure

Functional Information from GO Data
ChainGOidnamespacecontents
10000165biological_processMAPK cascade
10000278biological_processmitotic cell cycle
10001965molecular_functionG-protein alpha-subunit binding
10003723molecular_functionRNA binding
10004721molecular_functionphosphoprotein phosphatase activity
10004722molecular_functionprotein serine/threonine phosphatase activity
10005515molecular_functionprotein binding
10005524molecular_functionATP binding
10005634cellular_componentnucleus
10005654cellular_componentnucleoplasm
10005737cellular_componentcytoplasm
10005829cellular_componentcytosol
10005886cellular_componentplasma membrane
10006281biological_processDNA repair
10006302biological_processdouble-strand break repair
10006351biological_processDNA-templated transcription
10006974biological_processDNA damage response
10008017molecular_functionmicrotubule binding
10008289molecular_functionlipid binding
10010288biological_processresponse to lead ion
10016787molecular_functionhydrolase activity
10016791molecular_functionphosphatase activity
10030291molecular_functionprotein serine/threonine kinase inhibitor activity
10030544molecular_functionHsp70 protein binding
10031072molecular_functionheat shock protein binding
10031435molecular_functionmitogen-activated protein kinase kinase kinase binding
10032991cellular_componentprotein-containing complex
10042802molecular_functionidentical protein binding
10043025cellular_componentneuronal cell body
10043066biological_processnegative regulation of apoptotic process
10043123biological_processpositive regulation of canonical NF-kappaB signal transduction
10043204cellular_componentperikaryon
10043409biological_processnegative regulation of MAPK cascade
10043531molecular_functionADP binding
10044877molecular_functionprotein-containing complex binding
10046872molecular_functionmetal ion binding
10048156molecular_functiontau protein binding
10051879molecular_functionHsp90 protein binding
10070262biological_processpeptidyl-serine dephosphorylation
10070301biological_processcellular response to hydrogen peroxide
10071276biological_processcellular response to cadmium ion
10101031cellular_componentprotein folding chaperone complex
11904550biological_processresponse to arachidonate
11990635cellular_componentproximal dendrite
12000324biological_processpositive regulation of nuclear receptor-mediated glucocorticoid signaling pathway
20000165biological_processMAPK cascade
20000278biological_processmitotic cell cycle
20001965molecular_functionG-protein alpha-subunit binding
20003723molecular_functionRNA binding
20004721molecular_functionphosphoprotein phosphatase activity
20004722molecular_functionprotein serine/threonine phosphatase activity
20005515molecular_functionprotein binding
20005524molecular_functionATP binding
20005634cellular_componentnucleus
20005654cellular_componentnucleoplasm
20005737cellular_componentcytoplasm
20005829cellular_componentcytosol
20005886cellular_componentplasma membrane
20006281biological_processDNA repair
20006302biological_processdouble-strand break repair
20006351biological_processDNA-templated transcription
20006974biological_processDNA damage response
20008017molecular_functionmicrotubule binding
20008289molecular_functionlipid binding
20010288biological_processresponse to lead ion
20016787molecular_functionhydrolase activity
20016791molecular_functionphosphatase activity
20030291molecular_functionprotein serine/threonine kinase inhibitor activity
20030544molecular_functionHsp70 protein binding
20031072molecular_functionheat shock protein binding
20031435molecular_functionmitogen-activated protein kinase kinase kinase binding
20032991cellular_componentprotein-containing complex
20042802molecular_functionidentical protein binding
20043025cellular_componentneuronal cell body
20043066biological_processnegative regulation of apoptotic process
20043123biological_processpositive regulation of canonical NF-kappaB signal transduction
20043204cellular_componentperikaryon
20043409biological_processnegative regulation of MAPK cascade
20043531molecular_functionADP binding
20044877molecular_functionprotein-containing complex binding
20046872molecular_functionmetal ion binding
20048156molecular_functiontau protein binding
20051879molecular_functionHsp90 protein binding
20070262biological_processpeptidyl-serine dephosphorylation
20070301biological_processcellular response to hydrogen peroxide
20071276biological_processcellular response to cadmium ion
20101031cellular_componentprotein folding chaperone complex
21904550biological_processresponse to arachidonate
21990635cellular_componentproximal dendrite
22000324biological_processpositive regulation of nuclear receptor-mediated glucocorticoid signaling pathway
30000165biological_processMAPK cascade
30000278biological_processmitotic cell cycle
30001965molecular_functionG-protein alpha-subunit binding
30003723molecular_functionRNA binding
30004721molecular_functionphosphoprotein phosphatase activity
30004722molecular_functionprotein serine/threonine phosphatase activity
30005515molecular_functionprotein binding
30005524molecular_functionATP binding
30005634cellular_componentnucleus
30005654cellular_componentnucleoplasm
30005737cellular_componentcytoplasm
30005829cellular_componentcytosol
30005886cellular_componentplasma membrane
30006281biological_processDNA repair
30006302biological_processdouble-strand break repair
30006351biological_processDNA-templated transcription
30006974biological_processDNA damage response
30008017molecular_functionmicrotubule binding
30008289molecular_functionlipid binding
30010288biological_processresponse to lead ion
30016787molecular_functionhydrolase activity
30016791molecular_functionphosphatase activity
30030291molecular_functionprotein serine/threonine kinase inhibitor activity
30030544molecular_functionHsp70 protein binding
30031072molecular_functionheat shock protein binding
30031435molecular_functionmitogen-activated protein kinase kinase kinase binding
30032991cellular_componentprotein-containing complex
30042802molecular_functionidentical protein binding
30043025cellular_componentneuronal cell body
30043066biological_processnegative regulation of apoptotic process
30043123biological_processpositive regulation of canonical NF-kappaB signal transduction
30043204cellular_componentperikaryon
30043409biological_processnegative regulation of MAPK cascade
30043531molecular_functionADP binding
30044877molecular_functionprotein-containing complex binding
30046872molecular_functionmetal ion binding
30048156molecular_functiontau protein binding
30051879molecular_functionHsp90 protein binding
30070262biological_processpeptidyl-serine dephosphorylation
30070301biological_processcellular response to hydrogen peroxide
30071276biological_processcellular response to cadmium ion
30101031cellular_componentprotein folding chaperone complex
31904550biological_processresponse to arachidonate
31990635cellular_componentproximal dendrite
32000324biological_processpositive regulation of nuclear receptor-mediated glucocorticoid signaling pathway
40000165biological_processMAPK cascade
40000278biological_processmitotic cell cycle
40001965molecular_functionG-protein alpha-subunit binding
40003723molecular_functionRNA binding
40004721molecular_functionphosphoprotein phosphatase activity
40004722molecular_functionprotein serine/threonine phosphatase activity
40005515molecular_functionprotein binding
40005524molecular_functionATP binding
40005634cellular_componentnucleus
40005654cellular_componentnucleoplasm
40005737cellular_componentcytoplasm
40005829cellular_componentcytosol
40005886cellular_componentplasma membrane
40006281biological_processDNA repair
40006302biological_processdouble-strand break repair
40006351biological_processDNA-templated transcription
40006974biological_processDNA damage response
40008017molecular_functionmicrotubule binding
40008289molecular_functionlipid binding
40010288biological_processresponse to lead ion
40016787molecular_functionhydrolase activity
40016791molecular_functionphosphatase activity
40030291molecular_functionprotein serine/threonine kinase inhibitor activity
40030544molecular_functionHsp70 protein binding
40031072molecular_functionheat shock protein binding
40031435molecular_functionmitogen-activated protein kinase kinase kinase binding
40032991cellular_componentprotein-containing complex
40042802molecular_functionidentical protein binding
40043025cellular_componentneuronal cell body
40043066biological_processnegative regulation of apoptotic process
40043123biological_processpositive regulation of canonical NF-kappaB signal transduction
40043204cellular_componentperikaryon
40043409biological_processnegative regulation of MAPK cascade
40043531molecular_functionADP binding
40044877molecular_functionprotein-containing complex binding
40046872molecular_functionmetal ion binding
40048156molecular_functiontau protein binding
40051879molecular_functionHsp90 protein binding
40070262biological_processpeptidyl-serine dephosphorylation
40070301biological_processcellular response to hydrogen peroxide
40071276biological_processcellular response to cadmium ion
40101031cellular_componentprotein folding chaperone complex
41904550biological_processresponse to arachidonate
41990635cellular_componentproximal dendrite
42000324biological_processpositive regulation of nuclear receptor-mediated glucocorticoid signaling pathway
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MN 1 601
ChainResidue
1ASP271
1ASN303
1HIS352
1HIS427
1MN602

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MN 1 602
ChainResidue
1MN601
1ASP242
1HIS244
1ASP271
1TYR451

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MN 2 601
ChainResidue
2ASP242
2ASP271
2ASN303
2HIS352
2HIS427
2MN602

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MN 2 602
ChainResidue
2ASP242
2HIS244
2ASP271
2MN601

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MN 3 601
ChainResidue
3ASP242
3ASP271
3ASN303
3HIS352
3HIS427
3MN602

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MN 3 602
ChainResidue
3ASP242
3HIS244
3ASP271
3TYR451
3MN601

site_idAC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MN 4 601
ChainResidue
4ASP242
4ASP271
4ASN303
4HIS352
4HIS427
4MN602

site_idAC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MN 4 602
ChainResidue
4GLU76
4ASP242
4HIS244
4ASP271
4ARG275
4MN601

Functional Information from PROSITE/UniProt
site_idPS00125
Number of Residues6
DetailsSER_THR_PHOSPHATASE Serine/threonine specific protein phosphatases signature. LRGNHE
ChainResidueDetails
1LEU300-GLU305

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues132
DetailsRepeat: {"description":"TPR 1"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues132
DetailsRepeat: {"description":"TPR 2"}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues132
DetailsRepeat: {"description":"TPR 3"}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues630
DetailsRegion: {"description":"Catalytic"}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues8
DetailsRegion: {"description":"Required for autoinhibition","evidences":[{"source":"UniProtKB","id":"P53042","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues4
DetailsActive site: {"description":"Proton donor/acceptor","evidences":[{"source":"PubMed","id":"15155720","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues16
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"15155720","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15577939","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19601647","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1S95","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1WAO","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3H60","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3H61","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3H62","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3H63","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3H64","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues20
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"15155720","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1aui
ChainResidueDetails
1HIS304
1ASP274

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1aui
ChainResidueDetails
2HIS304
2ASP274

site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1aui
ChainResidueDetails
3HIS304
3ASP274

site_idCSA4
Number of Residues2
DetailsAnnotated By Reference To The Literature 1aui
ChainResidueDetails
4HIS304
4ASP274

site_idMCSA1
Number of Residues10
DetailsM-CSA 472
ChainResidueDetails

site_idMCSA2
Number of Residues10
DetailsM-CSA 472
ChainResidueDetails

site_idMCSA3
Number of Residues10
DetailsM-CSA 472
ChainResidueDetails

site_idMCSA4
Number of Residues10
DetailsM-CSA 472
ChainResidueDetails

245663

PDB entries from 2025-12-03

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