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6T58

Structure determination of the transactivation domain of p53 in complex with S100A4 using annexin A2 as a crystallization chaperone

Functional Information from GO Data
ChainGOidnamespacecontents
A0001525biological_processangiogenesis
A0001533cellular_componentcornified envelope
A0001765biological_processmembrane raft assembly
A0001786molecular_functionphosphatidylserine binding
A0001837biological_processepithelial to mesenchymal transition
A0001921biological_processpositive regulation of receptor recycling
A0002020molecular_functionprotease binding
A0002091biological_processnegative regulation of receptor internalization
A0003723molecular_functionRNA binding
A0003779molecular_functionactin binding
A0004859molecular_functionphospholipase inhibitor activity
A0004867molecular_functionserine-type endopeptidase inhibitor activity
A0005509molecular_functioncalcium ion binding
A0005515molecular_functionprotein binding
A0005544molecular_functioncalcium-dependent phospholipid binding
A0005546molecular_functionphosphatidylinositol-4,5-bisphosphate binding
A0005576cellular_componentextracellular region
A0005604cellular_componentbasement membrane
A0005615cellular_componentextracellular space
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0005737cellular_componentcytoplasm
A0005765cellular_componentlysosomal membrane
A0005768cellular_componentendosome
A0005769cellular_componentearly endosome
A0005811cellular_componentlipid droplet
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0005912cellular_componentadherens junction
A0006900biological_processvesicle budding from membrane
A0007155biological_processcell adhesion
A0007160biological_processcell-matrix adhesion
A0008092molecular_functioncytoskeletal protein binding
A0009986cellular_componentcell surface
A0010756biological_processpositive regulation of plasminogen activation
A0012506cellular_componentvesicle membrane
A0014823biological_processresponse to activity
A0016020cellular_componentmembrane
A0016323cellular_componentbasolateral plasma membrane
A0016363cellular_componentnuclear matrix
A0019834molecular_functionphospholipase A2 inhibitor activity
A0030199biological_processcollagen fibril organization
A0030324biological_processlung development
A0030496cellular_componentmidbody
A0031012cellular_componentextracellular matrix
A0031340biological_processpositive regulation of vesicle fusion
A0031902cellular_componentlate endosome membrane
A0031982cellular_componentvesicle
A0032804biological_processnegative regulation of low-density lipoprotein particle receptor catabolic process
A0035578cellular_componentazurophil granule lumen
A0035749cellular_componentmyelin sheath adaxonal region
A0036035biological_processosteoclast development
A0042056molecular_functionchemoattractant activity
A0042383cellular_componentsarcolemma
A0042470cellular_componentmelanosome
A0042730biological_processfibrinolysis
A0042789biological_processmRNA transcription by RNA polymerase II
A0042802molecular_functionidentical protein binding
A0043123biological_processpositive regulation of canonical NF-kappaB signal transduction
A0043220cellular_componentSchmidt-Lanterman incisure
A0044090biological_processpositive regulation of vacuole organization
A0044548molecular_functionS100 protein binding
A0045121cellular_componentmembrane raft
A0045921biological_processpositive regulation of exocytosis
A0045944biological_processpositive regulation of transcription by RNA polymerase II
A0046872molecular_functionmetal ion binding
A0046914molecular_functiontransition metal ion binding
A0048306molecular_functioncalcium-dependent protein binding
A0048471cellular_componentperinuclear region of cytoplasm
A0050767biological_processregulation of neurogenesis
A0050786molecular_functionRAGE receptor binding
A0050918biological_processpositive chemotaxis
A0051051biological_processnegative regulation of transport
A0051240biological_processpositive regulation of multicellular organismal process
A0070062cellular_componentextracellular exosome
A0090575cellular_componentRNA polymerase II transcription regulator complex
A0098609biological_processcell-cell adhesion
A0098641molecular_functioncadherin binding involved in cell-cell adhesion
A0098797cellular_componentplasma membrane protein complex
A1904019biological_processepithelial cell apoptotic process
A1905581biological_processpositive regulation of low-density lipoprotein particle clearance
A1905602biological_processpositive regulation of receptor-mediated endocytosis involved in cholesterol transport
A1905686biological_processpositive regulation of plasma membrane repair
A1990665cellular_componentAnxA2-p11 complex
A1990667cellular_componentPCSK9-AnxA2 complex
B0001525biological_processangiogenesis
B0001533cellular_componentcornified envelope
B0001765biological_processmembrane raft assembly
B0001786molecular_functionphosphatidylserine binding
B0001837biological_processepithelial to mesenchymal transition
B0001921biological_processpositive regulation of receptor recycling
B0002020molecular_functionprotease binding
B0002091biological_processnegative regulation of receptor internalization
B0003723molecular_functionRNA binding
B0003779molecular_functionactin binding
B0004859molecular_functionphospholipase inhibitor activity
B0004867molecular_functionserine-type endopeptidase inhibitor activity
B0005509molecular_functioncalcium ion binding
B0005515molecular_functionprotein binding
B0005544molecular_functioncalcium-dependent phospholipid binding
B0005546molecular_functionphosphatidylinositol-4,5-bisphosphate binding
B0005576cellular_componentextracellular region
B0005604cellular_componentbasement membrane
B0005615cellular_componentextracellular space
B0005634cellular_componentnucleus
B0005654cellular_componentnucleoplasm
B0005737cellular_componentcytoplasm
B0005765cellular_componentlysosomal membrane
B0005768cellular_componentendosome
B0005769cellular_componentearly endosome
B0005811cellular_componentlipid droplet
B0005829cellular_componentcytosol
B0005886cellular_componentplasma membrane
B0005912cellular_componentadherens junction
B0006900biological_processvesicle budding from membrane
B0007155biological_processcell adhesion
B0007160biological_processcell-matrix adhesion
B0008092molecular_functioncytoskeletal protein binding
B0009986cellular_componentcell surface
B0010756biological_processpositive regulation of plasminogen activation
B0012506cellular_componentvesicle membrane
B0014823biological_processresponse to activity
B0016020cellular_componentmembrane
B0016323cellular_componentbasolateral plasma membrane
B0016363cellular_componentnuclear matrix
B0019834molecular_functionphospholipase A2 inhibitor activity
B0030199biological_processcollagen fibril organization
B0030324biological_processlung development
B0030496cellular_componentmidbody
B0031012cellular_componentextracellular matrix
B0031340biological_processpositive regulation of vesicle fusion
B0031902cellular_componentlate endosome membrane
B0031982cellular_componentvesicle
B0032804biological_processnegative regulation of low-density lipoprotein particle receptor catabolic process
B0035578cellular_componentazurophil granule lumen
B0035749cellular_componentmyelin sheath adaxonal region
B0036035biological_processosteoclast development
B0042056molecular_functionchemoattractant activity
B0042383cellular_componentsarcolemma
B0042470cellular_componentmelanosome
B0042730biological_processfibrinolysis
B0042789biological_processmRNA transcription by RNA polymerase II
B0042802molecular_functionidentical protein binding
B0043123biological_processpositive regulation of canonical NF-kappaB signal transduction
B0043220cellular_componentSchmidt-Lanterman incisure
B0044090biological_processpositive regulation of vacuole organization
B0044548molecular_functionS100 protein binding
B0045121cellular_componentmembrane raft
B0045921biological_processpositive regulation of exocytosis
B0045944biological_processpositive regulation of transcription by RNA polymerase II
B0046872molecular_functionmetal ion binding
B0046914molecular_functiontransition metal ion binding
B0048306molecular_functioncalcium-dependent protein binding
B0048471cellular_componentperinuclear region of cytoplasm
B0050767biological_processregulation of neurogenesis
B0050786molecular_functionRAGE receptor binding
B0050918biological_processpositive chemotaxis
B0051051biological_processnegative regulation of transport
B0051240biological_processpositive regulation of multicellular organismal process
B0070062cellular_componentextracellular exosome
B0090575cellular_componentRNA polymerase II transcription regulator complex
B0098609biological_processcell-cell adhesion
B0098641molecular_functioncadherin binding involved in cell-cell adhesion
B0098797cellular_componentplasma membrane protein complex
B1904019biological_processepithelial cell apoptotic process
B1905581biological_processpositive regulation of low-density lipoprotein particle clearance
B1905602biological_processpositive regulation of receptor-mediated endocytosis involved in cholesterol transport
B1905686biological_processpositive regulation of plasma membrane repair
B1990665cellular_componentAnxA2-p11 complex
B1990667cellular_componentPCSK9-AnxA2 complex
Functional Information from PDB Data
site_idAC1
Number of Residues5
Detailsbinding site for residue GOL A 601
ChainResidue
ACYS359
AARG361
AARG405
ALEU485
ALYS492

site_idAC2
Number of Residues5
Detailsbinding site for residue GOL A 602
ChainResidue
AVAL524
APRO332
AASP336
AGLU365
ASER520

site_idAC3
Number of Residues5
Detailsbinding site for residue CA A 603
ChainResidue
AASP124
AASN126
AASP128
AGLU130
AGLU135

site_idAC4
Number of Residues4
Detailsbinding site for residue CA A 604
ChainResidue
AGLY428
AARG431
AGLY433
AGLU473

site_idAC5
Number of Residues3
Detailsbinding site for residue CA A 605
ChainResidue
AGLY276
AVAL277
AGLU279

site_idAC6
Number of Residues5
Detailsbinding site for residue CA A 606
ChainResidue
AMET344
AGLY346
ALEU347
AGLY348
AASP388

site_idAC7
Number of Residues7
Detailsbinding site for residue CA A 607
ChainResidue
AASP222
ASER223
AASN224
AARG225
AASP226
AGLU228
AGLU233

site_idAC8
Number of Residues2
Detailsbinding site for residue CA A 608
ChainResidue
ATHR349
AGLU351

site_idAC9
Number of Residues7
Detailsbinding site for residue CA A 609
ChainResidue
ASER179
AGLU182
AGLY183
AASP184
ALYS187
AASN189
AGLU192

site_idAD1
Number of Residues4
Detailsbinding site for residue CA A 610
ChainResidue
AMET504
AGLY506
AGLY508
AASP548

site_idAD2
Number of Residues4
Detailsbinding site for residue CA A 611
ChainResidue
ALYS314
ALEU317
AGLU322
BASP296

site_idAD3
Number of Residues5
Detailsbinding site for residue CA A 612
ChainResidue
ASER81
AGLU84
AASP86
ALYS89
AGLU94

site_idAD4
Number of Residues7
Detailsbinding site for residue GOL B 601
ChainResidue
BPRO332
BASP336
BARG361
BGLU365
BSER520
BARG521
BVAL524

site_idAD5
Number of Residues5
Detailsbinding site for residue GOL B 602
ChainResidue
BCYS359
BARG361
BASN363
BARG405
BLYS492

site_idAD6
Number of Residues5
Detailsbinding site for residue CA B 603
ChainResidue
BMET504
BGLY506
BGLY508
BTHR509
BASP548

site_idAD7
Number of Residues4
Detailsbinding site for residue CA B 604
ChainResidue
BMET344
BGLY346
BGLY348
BASP388

site_idAD8
Number of Residues1
Detailsbinding site for residue CA B 605
ChainResidue
BSER460

site_idAD9
Number of Residues5
Detailsbinding site for residue CA B 606
ChainResidue
BGLY428
BVAL429
BARG431
BGLY433
BGLU473

site_idAE1
Number of Residues3
Detailsbinding site for residue CA B 607
ChainResidue
BGLY276
BVAL277
BGLU279

site_idAE2
Number of Residues3
Detailsbinding site for residue CA B 608
ChainResidue
BLYS314
BLEU317
BGLU322

Functional Information from PROSITE/UniProt
site_idPS00018
Number of Residues13
DetailsEF_HAND_1 EF-hand calcium-binding domain. DSNRDNEVDfqEY
ChainResidueDetails
AASP124-TYR136
AASP222-TYR234

site_idPS00223
Number of Residues53
DetailsANNEXIN_1 Annexin repeat signature. GVdevtivniLtnRsneQrqDiafaYqrrtkkeLasaLksalsGhletvIlgL
ChainResidueDetails
AGLY276-LEU328
AGLY348-LEU400
AGLY433-LEU485
AGLY508-LEU560

site_idPS00303
Number of Residues22
DetailsS100_CABP S-100/ICaBP type calcium binding protein signature. LMsnLDsnrDnevDFqEYcvFL
ChainResidueDetails
ALEU119-LEU140
ALEU217-LEU238

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsMOD_RES: Phosphothreonine; by CK1, VRK1 and VRK2 => ECO:0000269|PubMed:10606744, ECO:0000269|PubMed:10951572, ECO:0000269|PubMed:16704422, ECO:0000269|PubMed:31527692
ChainResidueDetails
ATHR18
BTHR18

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: Phosphoserine; by CHEK2, CK1 and PLK3 => ECO:0000269|PubMed:10570149, ECO:0000269|PubMed:11447225, ECO:0000269|PubMed:11551930, ECO:0000269|PubMed:12810724, ECO:0000269|PubMed:20041275
ChainResidueDetails
ASER20
BSER20

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: Phosphoserine; by CDK5 and CDK7 => ECO:0000269|PubMed:17591690, ECO:0000269|PubMed:9372954
ChainResidueDetails
ASER33
BSER33

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphoserine; by MAPKAPK5 => ECO:0000269|PubMed:17254968
ChainResidueDetails
ASER37
BSER37

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Phosphoserine; by CDK5, DYRK2, HIPK2 and PKC/PRKCG => ECO:0000269|PubMed:11740489, ECO:0000269|PubMed:11780126, ECO:0000269|PubMed:16377624, ECO:0000269|PubMed:17349958, ECO:0000269|PubMed:17591690
ChainResidueDetails
ASER46
BSER46

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: Phosphothreonine; by TAF1 and GRK5 => ECO:0000269|PubMed:15053879, ECO:0000269|PubMed:20124405
ChainResidueDetails
ATHR55
BTHR55

site_idSWS_FT_FI7
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:21597459
ChainResidueDetails
ALYS24
BLYS24

site_idSWS_FT_FI8
Number of Residues4
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0007744|PubMed:28112733
ChainResidueDetails
ALYS275
BLYS275

site_idSWS_FT_FI9
Number of Residues4
DetailsBINDING: BINDING => ECO:0000305
ChainResidueDetails
ALYS187
AGLU192
BLYS187
BGLU192

site_idSWS_FT_FI10
Number of Residues10
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00448
ChainResidueDetails
AASP222
BGLU233
AASN224
AASP226
AGLU228
AGLU233
BASP222
BASN224
BASP226
BGLU228

site_idSWS_FT_FI11
Number of Residues2
DetailsMOD_RES: N-acetylalanine => ECO:0000250|UniProtKB:P35466
ChainResidueDetails
AALA161
BALA161

site_idSWS_FT_FI12
Number of Residues4
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861
ChainResidueDetails
ALYS166
ALYS194
BLYS166
BLYS194

site_idSWS_FT_FI13
Number of Residues2
DetailsMOD_RES: Phosphoserine; by PKC => ECO:0000269|PubMed:28669632, ECO:0000269|PubMed:2946940
ChainResidueDetails
APHE252
BPHE252

site_idSWS_FT_FI14
Number of Residues2
DetailsMOD_RES: N6-acetyllysine; alternate => ECO:0000250|UniProtKB:P07356
ChainResidueDetails
ALYS275
BLYS275

site_idSWS_FT_FI15
Number of Residues4
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P07356
ChainResidueDetails
ALYS378
ALYS453
BLYS378
BLYS453

site_idSWS_FT_FI16
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER410
BSER410

site_idSWS_FT_FI17
Number of Residues2
DetailsMOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P07356
ChainResidueDetails
ATYR425
BTYR425

237735

PDB entries from 2025-06-18

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