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6FI4

Crystal structure of C-terminal modified Tau peptide-hybrid 3.2e with 14-3-3sigma

Functional Information from GO Data
ChainGOidnamespacecontents
A0000122biological_processnegative regulation of transcription by RNA polymerase II
A0001836biological_processrelease of cytochrome c from mitochondria
A0003334biological_processkeratinocyte development
A0005515molecular_functionprotein binding
A0005576cellular_componentextracellular region
A0005615cellular_componentextracellular space
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006469biological_processnegative regulation of protein kinase activity
A0006611biological_processprotein export from nucleus
A0007165biological_processsignal transduction
A0008104biological_processprotein localization
A0008426molecular_functionprotein kinase C inhibitor activity
A0008630biological_processintrinsic apoptotic signaling pathway in response to DNA damage
A0010482biological_processregulation of epidermal cell division
A0010839biological_processnegative regulation of keratinocyte proliferation
A0019901molecular_functionprotein kinase binding
A0022407biological_processregulation of cell-cell adhesion
A0030216biological_processkeratinocyte differentiation
A0030307biological_processpositive regulation of cell growth
A0031424biological_processkeratinization
A0032880biological_processregulation of protein localization
A0042742biological_processdefense response to bacterium
A0042802molecular_functionidentical protein binding
A0043588biological_processskin development
A0043616biological_processkeratinocyte proliferation
A0045296molecular_functioncadherin binding
A0045606biological_processpositive regulation of epidermal cell differentiation
A0045785biological_processpositive regulation of cell adhesion
A0045824biological_processnegative regulation of innate immune response
A0046827biological_processpositive regulation of protein export from nucleus
A0050815molecular_functionphosphoserine residue binding
A0051219molecular_functionphosphoprotein binding
A0051715biological_processcytolysis in another organism
A0051726biological_processregulation of cell cycle
A0061436biological_processestablishment of skin barrier
A0070062cellular_componentextracellular exosome
A0072089biological_processstem cell proliferation
A0140311molecular_functionprotein sequestering activity
A0141156biological_processcAMP/PKA signal transduction
A0160075biological_processnon-canonical inflammasome complex assembly
A1903077biological_processnegative regulation of protein localization to plasma membrane
A1903829biological_processpositive regulation of protein localization
A2000647biological_processnegative regulation of stem cell proliferation
Functional Information from PDB Data
site_idAC1
Number of Residues6
Detailsbinding site for residue CA A 301
ChainResidue
AALA203
AASP204
AHOH442
AHOH442
AHOH481
AHOH486

site_idAC2
Number of Residues2
Detailsbinding site for residue CL A 302
ChainResidue
ALYS9
AHOH516

site_idAC3
Number of Residues6
Detailsbinding site for residue NA A 303
ChainResidue
AGLU2
AHOH436
AHOH454
AHOH506
AHOH525
AGLY-1

site_idAC4
Number of Residues8
Detailsbinding site for residue 60H B 101
ChainResidue
ASER45
APHE119
ALYS122
AILE168
AASP215
BLEU6
BPRO7
BDVA8

Functional Information from PROSITE/UniProt
site_idPS00796
Number of Residues11
Details1433_1 14-3-3 proteins signature 1. RNLLSVAYKNV
ChainResidueDetails
AARG41-VAL51

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsMOD_RES: Phosphoserine; by PKA => ECO:0000269|PubMed:15546861, ECO:0000269|PubMed:16443603, ECO:0000269|PubMed:19451179, ECO:0000269|PubMed:9614189
ChainResidueDetails
BSEP5
AARG129

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:20068231
ChainResidueDetails
ASER5

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER74

237423

PDB entries from 2025-06-11

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