Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

6TCH

Binary complex of 14-3-3 sigma and a high-affinity non-canonical 9-mer peptide binder

Functional Information from GO Data
ChainGOidnamespacecontents
B0000122biological_processnegative regulation of transcription by RNA polymerase II
B0001836biological_processrelease of cytochrome c from mitochondria
B0003334biological_processkeratinocyte development
B0005515molecular_functionprotein binding
B0005576cellular_componentextracellular region
B0005615cellular_componentextracellular space
B0005634cellular_componentnucleus
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006469biological_processnegative regulation of protein kinase activity
B0006611biological_processprotein export from nucleus
B0007165biological_processsignal transduction
B0008104biological_processprotein localization
B0008426molecular_functionprotein kinase C inhibitor activity
B0008630biological_processintrinsic apoptotic signaling pathway in response to DNA damage
B0010482biological_processregulation of epidermal cell division
B0010737biological_processprotein kinase A signaling
B0010839biological_processnegative regulation of keratinocyte proliferation
B0019901molecular_functionprotein kinase binding
B0022407biological_processregulation of cell-cell adhesion
B0030216biological_processkeratinocyte differentiation
B0030307biological_processpositive regulation of cell growth
B0031424biological_processkeratinization
B0032880biological_processregulation of protein localization
B0042802molecular_functionidentical protein binding
B0043588biological_processskin development
B0043616biological_processkeratinocyte proliferation
B0045296molecular_functioncadherin binding
B0045606biological_processpositive regulation of epidermal cell differentiation
B0045785biological_processpositive regulation of cell adhesion
B0045824biological_processnegative regulation of innate immune response
B0046827biological_processpositive regulation of protein export from nucleus
B0050815molecular_functionphosphoserine residue binding
B0051219molecular_functionphosphoprotein binding
B0051726biological_processregulation of cell cycle
B0061436biological_processestablishment of skin barrier
B0070062cellular_componentextracellular exosome
B0072089biological_processstem cell proliferation
B0140311molecular_functionprotein sequestering activity
B1903077biological_processnegative regulation of protein localization to plasma membrane
B1903829biological_processpositive regulation of protein localization
B2000647biological_processnegative regulation of stem cell proliferation
Functional Information from PDB Data
site_idAC1
Number of Residues3
Detailsbinding site for residue MG B 301
ChainResidue
BSER37
BGLU39
BHOH696

site_idAC2
Number of Residues8
Detailsbinding site for residue MG B 302
ChainResidue
BHOH705
BHOH705
BGLU2
BGLU2
BHOH424
BHOH424
BHOH620
BHOH620

site_idAC3
Number of Residues6
Detailsbinding site for residue MG B 303
ChainResidue
BGLU35
BGLU110
BGLU188
BHOH562
BHOH569
BHOH601

site_idAC4
Number of Residues4
Detailsbinding site for residue MG B 304
ChainResidue
BGLU75
BGLU161
BHOH554
BHOH573

site_idAC5
Number of Residues2
Detailsbinding site for residue CL B 305
ChainResidue
BLYS9
BHOH684

site_idAC6
Number of Residues8
Detailsbinding site for residues NVA A 1 and PPN A 2
ChainResidue
AKCJ3
ASEP4
AHOH109
BARG56
BALA57
BARG60
BHOH466
BHOH539

site_idAC7
Number of Residues13
Detailsbinding site for residues PPN A 2 and KCJ A 3
ChainResidue
ANVA1
ASEP4
AHOH105
AHOH109
BARG56
BALA57
BARG60
BLEU174
BVAL178
BGLU182
BASN226
BLEU229
BHOH539

site_idAC8
Number of Residues18
Detailsbinding site for residues KCJ A 3 and SEP A 4
ChainResidue
ANVA1
APPN2
APPN5
AHOH101
AHOH104
AHOH105
AHOH106
AHOH108
AHOH109
BARG56
BARG129
BTYR130
BLEU174
BASN175
BVAL178
BGLU182
BASN226
BLEU229

site_idAC9
Number of Residues19
Detailsbinding site for residues SEP A 4 and PPN A 5
ChainResidue
APPN2
AKCJ3
AB3S6
ABAL7
APPN8
AHOH101
AHOH104
AHOH105
AHOH106
AHOH108
AHOH109
BARG56
BLYS122
BARG129
BTYR130
BLEU174
BASN175
BILE219
BLEU222

site_idAD1
Number of Residues13
Detailsbinding site for residues PPN A 5 and B3S A 6
ChainResidue
ASEP4
ABAL7
APPN8
AHOH101
AHOH102
AHOH103
AHOH110
BSER45
BLYS122
BLEU174
BASN175
BILE219
BLEU222

site_idAD2
Number of Residues9
Detailsbinding site for residues B3S A 6 and BAL A 7
ChainResidue
AHOH110
BASN42
BSER45
BLYS122
APPN5
APPN8
AHOH101
AHOH102
AHOH103

site_idAD3
Number of Residues11
Detailsbinding site for residues BAL A 7 and PPN A 8
ChainResidue
APPN5
AB3S6
ALYS9
ANH210
AHOH103
BASN42
BSER45
BPHE119
BLYS122
BPRO167
BGLY171

Functional Information from PROSITE/UniProt
site_idPS00796
Number of Residues11
Details1433_1 14-3-3 proteins signature 1. RNLLSVAYKNV
ChainResidueDetails
BARG41-VAL51

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsSITE: Interaction with phosphoserine on interacting protein
ChainResidueDetails
BARG56
BARG129

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:20068231
ChainResidueDetails
BSER5

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
BSER74

222926

PDB entries from 2024-07-24

PDB statisticsPDBj update infoContact PDBjnumon