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4RAF

Crystal structure of PP2Ca-D38A

Functional Information from GO Data
ChainGOidnamespacecontents
A0000122biological_processnegative regulation of transcription by RNA polymerase II
A0000287molecular_functionmagnesium ion binding
A0004721molecular_functionphosphoprotein phosphatase activity
A0004722molecular_functionprotein serine/threonine phosphatase activity
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0006470biological_processprotein dephosphorylation
A0006499biological_processN-terminal protein myristoylation
A0006611biological_processprotein export from nucleus
A0016020cellular_componentmembrane
A0016311biological_processdephosphorylation
A0017018molecular_functionmyosin phosphatase activity
A0030145molecular_functionmanganese ion binding
A0030512biological_processnegative regulation of transforming growth factor beta receptor signaling pathway
A0030514biological_processnegative regulation of BMP signaling pathway
A0033192molecular_functioncalmodulin-dependent protein phosphatase activity
A0035970biological_processpeptidyl-threonine dephosphorylation
A0043123biological_processpositive regulation of canonical NF-kappaB signal transduction
A0043124biological_processnegative regulation of canonical NF-kappaB signal transduction
A0043169molecular_functioncation binding
A0045893biological_processpositive regulation of DNA-templated transcription
A0046827biological_processpositive regulation of protein export from nucleus
A0046872molecular_functionmetal ion binding
A0051726biological_processregulation of cell cycle
A0070412molecular_functionR-SMAD binding
A0071560biological_processcellular response to transforming growth factor beta stimulus
A0090263biological_processpositive regulation of canonical Wnt signaling pathway
A1901223biological_processnegative regulation of non-canonical NF-kappaB signal transduction
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MN A 401
ChainResidue
AASP60
AASP239
AASP282
AHOH509
AHOH534
AHOH557

Functional Information from PROSITE/UniProt
site_idPS01032
Number of Residues9
DetailsPPM_1 PPM-type phosphatase domain signature. FFAVYDGHA
ChainResidueDetails
APHE55-ALA63

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:9003755, ECO:0007744|PDB:1A6Q
ChainResidueDetails
AASP60
AGLY61
AASP239
AASP282

site_idSWS_FT_FI2
Number of Residues1
DetailsLIPID: N-myristoyl glycine => ECO:0000269|PubMed:20213681, ECO:0000269|PubMed:25255805
ChainResidueDetails
AGLY2

226707

PDB entries from 2024-10-30

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