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6RL4

Fragment AZ-025 binding at the p53pT387/14-3-3 sigma interface

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
A0010737biological_processprotein kinase A signaling
A0010839biological_processnegative regulation of keratinocyte proliferation
A0019901molecular_functionprotein kinase binding
A0030216biological_processkeratinocyte differentiation
A0030307biological_processpositive regulation of cell growth
A0031424biological_processkeratinization
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
A0051726biological_processregulation of cell cycle
A0061436biological_processestablishment of skin barrier
A0070062cellular_componentextracellular exosome
A0072089biological_processstem cell proliferation
A0140311molecular_functionprotein sequestering activity
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 Residues4
Detailsbinding site for residue MG A 301
ChainResidue
AGLU35
AGLU188
AHOH636
AHOH669

site_idAC2
Number of Residues5
Detailsbinding site for residue MG A 302
ChainResidue
AGLU86
AGLU89
AHOH417
AHOH615
AHOH621

site_idAC3
Number of Residues3
Detailsbinding site for residue CL A 303
ChainResidue
ALYS9
AHOH619
AHOH665

site_idAC4
Number of Residues8
Detailsbinding site for residue K7N A 304
ChainResidue
AGLU14
ACSO38
AGLU39
ALEU43
AASP215
AHOH404
AHOH430
AHOH553

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

site_idPS00797
Number of Residues20
Details1433_2 14-3-3 proteins signature 2. YKDSTLIMQLLRDNLTLWTA
ChainResidueDetails
ATYR213-ALA232

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsMOD_RES: N6-methyllysine; by KMT5A; alternate => ECO:0000269|PubMed:17707234, ECO:0000269|PubMed:20870725, ECO:0000269|PubMed:22864287
ChainResidueDetails
PLYS382
AARG129

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: Phosphoserine; by CK2, CDK2 and NUAK1 => ECO:0000269|PubMed:10884347, ECO:0000269|PubMed:11239457, ECO:0000269|PubMed:17108107, ECO:0000269|PubMed:21317932, ECO:0000269|PubMed:22214662
ChainResidueDetails
PSER392

site_idSWS_FT_FI3
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) => ECO:0000269|PubMed:11124955, ECO:0000269|PubMed:22214662, ECO:0000269|Ref.37
ChainResidueDetails
PLYS386

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:16964243, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:20068231
ChainResidueDetails
ASER248

219515

PDB entries from 2024-05-08

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