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5M36

The molecular tweezer CLR01 stabilizes a disordered protein-protein interface

Replaces:  5JIV
Functional Information from GO Data
ChainGOidnamespacecontents
A0000122biological_processnegative regulation of transcription by RNA polymerase II
A0001525biological_processangiogenesis
A0003016biological_processrespiratory system process
A0003723molecular_functionRNA binding
A0005515molecular_functionprotein binding
A0005615cellular_componentextracellular space
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0005925cellular_componentfocal adhesion
A0006468biological_processprotein phosphorylation
A0006605biological_processprotein targeting
A0007165biological_processsignal transduction
A0008039biological_processsynaptic target recognition
A0008104biological_processprotein localization
A0019901molecular_functionprotein kinase binding
A0019904molecular_functionprotein domain specific binding
A0030324biological_processlung development
A0031625molecular_functionubiquitin protein ligase binding
A0031647biological_processregulation of protein stability
A0031982cellular_componentvesicle
A0035148biological_processtube formation
A0042149biological_processcellular response to glucose starvation
A0042470cellular_componentmelanosome
A0042802molecular_functionidentical protein binding
A0043066biological_processnegative regulation of apoptotic process
A0043067biological_processregulation of programmed cell death
A0044325molecular_functiontransmembrane transporter binding
A0045296molecular_functioncadherin binding
A0045824biological_processnegative regulation of innate immune response
A0050815molecular_functionphosphoserine residue binding
A0051683biological_processestablishment of Golgi localization
A0070062cellular_componentextracellular exosome
A0070371biological_processERK1 and ERK2 cascade
A0070372biological_processregulation of ERK1 and ERK2 cascade
A0072562cellular_componentblood microparticle
A0090128biological_processregulation of synapse maturation
A0090168biological_processGolgi reassembly
A0098686cellular_componenthippocampal mossy fiber to CA3 synapse
A0098978cellular_componentglutamatergic synapse
A0140297molecular_functionDNA-binding transcription factor binding
A0140311molecular_functionprotein sequestering activity
A1900181biological_processnegative regulation of protein localization to nucleus
A1904262biological_processnegative regulation of TORC1 signaling
B0000122biological_processnegative regulation of transcription by RNA polymerase II
B0001525biological_processangiogenesis
B0003016biological_processrespiratory system process
B0003723molecular_functionRNA binding
B0005515molecular_functionprotein binding
B0005615cellular_componentextracellular space
B0005634cellular_componentnucleus
B0005654cellular_componentnucleoplasm
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0005925cellular_componentfocal adhesion
B0006468biological_processprotein phosphorylation
B0006605biological_processprotein targeting
B0007165biological_processsignal transduction
B0008039biological_processsynaptic target recognition
B0008104biological_processprotein localization
B0019901molecular_functionprotein kinase binding
B0019904molecular_functionprotein domain specific binding
B0030324biological_processlung development
B0031625molecular_functionubiquitin protein ligase binding
B0031647biological_processregulation of protein stability
B0031982cellular_componentvesicle
B0035148biological_processtube formation
B0042149biological_processcellular response to glucose starvation
B0042470cellular_componentmelanosome
B0042802molecular_functionidentical protein binding
B0043066biological_processnegative regulation of apoptotic process
B0043067biological_processregulation of programmed cell death
B0044325molecular_functiontransmembrane transporter binding
B0045296molecular_functioncadherin binding
B0045824biological_processnegative regulation of innate immune response
B0050815molecular_functionphosphoserine residue binding
B0051683biological_processestablishment of Golgi localization
B0070062cellular_componentextracellular exosome
B0070371biological_processERK1 and ERK2 cascade
B0070372biological_processregulation of ERK1 and ERK2 cascade
B0072562cellular_componentblood microparticle
B0090128biological_processregulation of synapse maturation
B0090168biological_processGolgi reassembly
B0098686cellular_componenthippocampal mossy fiber to CA3 synapse
B0098978cellular_componentglutamatergic synapse
B0140297molecular_functionDNA-binding transcription factor binding
B0140311molecular_functionprotein sequestering activity
B1900181biological_processnegative regulation of protein localization to nucleus
B1904262biological_processnegative regulation of TORC1 signaling
C0004725molecular_functionprotein tyrosine phosphatase activity
C0006470biological_processprotein dephosphorylation
C1902751biological_processpositive regulation of cell cycle G2/M phase transition
D0004725molecular_functionprotein tyrosine phosphatase activity
D0006470biological_processprotein dephosphorylation
D1902751biological_processpositive regulation of cell cycle G2/M phase transition
Functional Information from PDB Data
site_idAC1
Number of Residues5
Detailsbinding site for residue 9SZ A 301
ChainResidue
AARG60
ASER64
AGLN67
ATYR179
A9SZ302

site_idAC2
Number of Residues6
Detailsbinding site for residue 9SZ A 302
ChainResidue
BTYR178
BSER190
AASN183
A9SZ301
AHOH401
BGLN150

site_idAC3
Number of Residues2
Detailsbinding site for residue GOL A 305
ChainResidue
ALYS193
AASP197

site_idAC4
Number of Residues6
Detailsbinding site for residue 9SZ B 301
ChainResidue
AGLN150
ATYR178
ALYS187
BASN183
BHOH411
C9SZ301

site_idAC5
Number of Residues2
Detailsbinding site for residue GOL B 303
ChainResidue
BTYR82
BLYS85

site_idAC6
Number of Residues9
Detailsbinding site for residue 9SZ C 301
ChainResidue
BARG60
BGLN67
BTYR179
BGLU180
B9SZ301
CARG208
CSER209
CTYR212
CHOH408

site_idAC7
Number of Residues20
Detailsbinding site for residues BEZ A 303 and BEZ B 302
ChainResidue
AASN183
AMET218
AMET218
AGLN219
AARG222
AARG222
A9SZ301
AHOH401
BTYR82
BLYS85
BGLN150
BTYR178
BSER190
BPHE196
BPHE196
BMET218
BMET218
BGLN219
BARG222
BARG222

site_idAC8
Number of Residues20
Detailsbinding site for residues BEZ A 303 and BEZ B 302
ChainResidue
AASN183
AMET218
AMET218
AGLN219
AARG222
AARG222
A9SZ301
AHOH401
BTYR82
BLYS85
BGLN150
BTYR178
BSER190
BPHE196
BPHE196
BMET218
BMET218
BGLN219
BARG222
BARG222

site_idAC9
Number of Residues20
Detailsbinding site for residues BEZ A 303 and BEZ B 302
ChainResidue
AASN183
AMET218
AMET218
AGLN219
AARG222
AARG222
A9SZ301
AHOH401
BTYR82
BLYS85
BGLN150
BTYR178
BSER190
BPHE196
BPHE196
BMET218
BMET218
BGLN219
BARG222
BARG222

site_idAD1
Number of Residues20
Detailsbinding site for residues BEZ A 303 and BEZ B 302
ChainResidue
BLYS85
BGLN150
BTYR178
BSER190
BPHE196
BPHE196
BMET218
BMET218
BGLN219
BARG222
BARG222
AASN183
AMET218
AMET218
AGLN219
AARG222
AARG222
A9SZ301
AHOH401
BTYR82

site_idAD2
Number of Residues20
Detailsbinding site for residues BEZ A 303 and BEZ B 302
ChainResidue
AASN183
AMET218
AMET218
AGLN219
AARG222
AARG222
A9SZ301
AHOH401
BTYR82
BLYS85
BGLN150
BTYR178
BSER190
BPHE196
BPHE196
BMET218
BMET218
BGLN219
BARG222
BARG222

site_idAD3
Number of Residues20
Detailsbinding site for residues BEZ A 303 and BEZ B 302
ChainResidue
AASN183
AMET218
AMET218
AGLN219
AARG222
AARG222
A9SZ301
AHOH401
BTYR82
BLYS85
BGLN150
BTYR178
BSER190
BPHE196
BPHE196
BMET218
BMET218
BGLN219
BARG222
BARG222

site_idAD4
Number of Residues20
Detailsbinding site for residues BEZ A 303 and BEZ B 302
ChainResidue
AASN183
AMET218
AMET218
AGLN219
AARG222
AARG222
A9SZ301
AHOH401
BTYR82
BLYS85
BGLN150
BTYR178
BSER190
BPHE196
BPHE196
BMET218
BMET218
BGLN219
BARG222
BARG222

site_idAD5
Number of Residues20
Detailsbinding site for residues BEZ A 303 and BEZ B 302
ChainResidue
AASN183
AMET218
AMET218
AGLN219
AARG222
AARG222
A9SZ301
AHOH401
BTYR82
BLYS85
BGLN150
BTYR178
BSER190
BPHE196
BPHE196
BMET218
BMET218
BGLN219
BARG222
BARG222

site_idAD6
Number of Residues20
Detailsbinding site for residues BEZ A 303 and BEZ B 302
ChainResidue
AASN183
AMET218
AMET218
AGLN219
AARG222
AARG222
A9SZ301
AHOH401
BTYR82
BLYS85
BGLN150
BTYR178
BSER190
BPHE196
BPHE196
BMET218
BMET218
BGLN219
BARG222
BARG222

site_idAD7
Number of Residues20
Detailsbinding site for residues BEZ A 303 and BEZ B 302
ChainResidue
AASN183
AMET218
AMET218
AGLN219
AARG222
AARG222
A9SZ301
AHOH401
BTYR82
BLYS85
BGLN150
BTYR178
BSER190
BPHE196
BPHE196
BMET218
BMET218
BGLN219
BARG222
BARG222

site_idAD8
Number of Residues20
Detailsbinding site for residues BEZ A 303 and BEZ B 302
ChainResidue
AASN183
AMET218
AMET218
AGLN219
AARG222
AARG222
A9SZ301
AHOH401
BTYR82
BLYS85
BGLN150
BTYR178
BSER190
BPHE196
BPHE196
BMET218
BMET218
BGLN219
BARG222
BARG222

site_idAD9
Number of Residues20
Detailsbinding site for residues BEZ A 303 and BEZ B 302
ChainResidue
AASN183
AMET218
AMET218
AGLN219
AARG222
AARG222
A9SZ301
AHOH401
BTYR82
BLYS85
BGLN150
BTYR178
BSER190
BPHE196
BPHE196
BMET218
BMET218
BGLN219
BARG222
BARG222

site_idAE1
Number of Residues20
Detailsbinding site for residues BEZ A 303 and BEZ B 302
ChainResidue
AASN183
AMET218
AMET218
AGLN219
AARG222
AARG222
A9SZ301
AHOH401
BTYR82
BLYS85
BGLN150
BTYR178
BSER190
BPHE196
BPHE196
BMET218
BMET218
BGLN219
BARG222
BARG222

site_idAE2
Number of Residues20
Detailsbinding site for residues BEZ A 303 and BEZ B 302
ChainResidue
AASN183
AMET218
AMET218
AGLN219
AARG222
AARG222
A9SZ301
AHOH401
BTYR82
BLYS85
BGLN150
BTYR178
BSER190
BPHE196
BPHE196
BMET218
BMET218
BGLN219
BARG222
BARG222

site_idAE3
Number of Residues20
Detailsbinding site for residues BEZ A 303 and BEZ B 302
ChainResidue
AASN183
AMET218
AMET218
AGLN219
AARG222
AARG222
A9SZ301
AHOH401
BTYR82
BLYS85
BGLN150
BTYR178
BSER190
BPHE196
BPHE196
BMET218
BMET218
BGLN219
BARG222
BARG222

site_idAE4
Number of Residues20
Detailsbinding site for residues BEZ A 303 and BEZ B 302
ChainResidue
AASN183
AMET218
AMET218
AGLN219
AARG222
AARG222
A9SZ301
AHOH401
BTYR82
BLYS85
BGLN150
BTYR178
BSER190
BPHE196
BPHE196
BMET218
BMET218
BGLN219
BARG222
BARG222

site_idAE5
Number of Residues20
Detailsbinding site for residues BEZ A 303 and BEZ B 302
ChainResidue
AASN183
AMET218
AMET218
AGLN219
AARG222
AARG222
A9SZ301
AHOH401
BTYR82
BLYS85
BGLN150
BTYR178
BSER190
BPHE196
BPHE196
BMET218
BMET218
BGLN219
BARG222
BARG222

site_idAE6
Number of Residues20
Detailsbinding site for residues BEZ A 303 and BEZ B 302
ChainResidue
AASN183
AMET218
AMET218
AGLN219
AARG222
AARG222
A9SZ301
AHOH401
BTYR82
BLYS85
BGLN150
BTYR178
BSER190
BPHE196
BPHE196
BMET218
BMET218
BGLN219
BARG222
BARG222

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. YKDSTLIMQLLRDNLTLWTS
ChainResidueDetails
ATYR211-SER230

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsMOD_RES: Phosphoserine; by CDK1 => ECO:0000305|PubMed:8119945
ChainResidueDetails
CSER214
DSER214
BARG56
BARG127

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: Phosphoserine; by CHEK1, CHEK2, BRSK1, MAPK14 AND MARK3 => ECO:0000269|PubMed:11333986, ECO:0000269|PubMed:15150265, ECO:0000269|PubMed:15629715, ECO:0007744|PubMed:23186163
ChainResidueDetails
CSEP216
DSEP216
BLYS3
BLYS68

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: Phosphoserine; by PKA and PKB/AKT1 => ECO:0000269|PubMed:11956222, ECO:0000269|PubMed:12865427, ECO:0000269|PubMed:15883165, ECO:0000269|PubMed:16376338
ChainResidueDetails
ASER58
BSER58

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphoserine; by MAPK8 => ECO:0000269|PubMed:15071501, ECO:0000269|PubMed:15696159
ChainResidueDetails
ASER184
BSER184

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231
ChainResidueDetails
ASER207
BSER207

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P63102
ChainResidueDetails
ASER210
BSER210

220472

PDB entries from 2024-05-29

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