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5LPX

Crystal structure of PKC phosphorylation-mimicking mutant (S26E) Annexin A2

Functional Information from GO Data
ChainGOidnamespacecontents
A0001525biological_processangiogenesis
A0001533cellular_componentcornified envelope
A0001765biological_processmembrane raft assembly
A0001786molecular_functionphosphatidylserine binding
A0001921biological_processpositive regulation of receptor recycling
A0002020molecular_functionprotease binding
A0002091biological_processnegative regulation of receptor internalization
A0003723molecular_functionRNA 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
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
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
A0042383cellular_componentsarcolemma
A0042470cellular_componentmelanosome
A0042730biological_processfibrinolysis
A0042789biological_processmRNA transcription by RNA polymerase II
A0042802molecular_functionidentical protein binding
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
A0048306molecular_functioncalcium-dependent protein binding
A0050767biological_processregulation of neurogenesis
A0062023cellular_componentcollagen-containing extracellular matrix
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
A1905597biological_processpositive regulation of low-density lipoprotein particle receptor binding
A1905599biological_processpositive regulation of low-density lipoprotein receptor activity
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
Functional Information from PDB Data
site_idAC1
Number of Residues7
Detailsbinding site for residue CA A 401
ChainResidue
AGLY50
AVAL51
AGLU53
AHOH722
AHOH799
AHOH842
AHOH850

site_idAC2
Number of Residues7
Detailsbinding site for residue CA A 402
ChainResidue
AGLU96
AHOH801
AHOH813
AHOH863
AHOH885
ALYS88
ALEU91

site_idAC3
Number of Residues6
Detailsbinding site for residue CA A 403
ChainResidue
AMET118
AGLY120
AGLY122
AASP162
AHOH536
AHOH699

site_idAC4
Number of Residues6
Detailsbinding site for residue CA A 404
ChainResidue
AGLY202
AARG205
AGLY207
AGLU247
AHOH715
AHOH840

site_idAC5
Number of Residues4
Detailsbinding site for residue CA A 405
ChainResidue
AMET278
AGLY280
AGLY282
AASP322

site_idAC6
Number of Residues7
Detailsbinding site for residue GOL A 406
ChainResidue
ACYS133
ASER134
AARG135
AARG179
ALYS266
AHOH532
AHOH629

site_idAC7
Number of Residues9
Detailsbinding site for residue GOL A 407
ChainResidue
AALA180
AGLU181
AGLY183
AARG220
ASER221
AHIS224
AHOH512
AHOH528
AHOH585

Functional Information from PROSITE/UniProt
site_idPS00223
Number of Residues53
DetailsANNEXIN_1 Annexin repeat signature. GVdevtivniLtnRsneQrqDiafaYqrrtkkeLasaLksalsGhletvIlgL
ChainResidueDetails
AGLY50-LEU102
AGLY122-LEU174
AGLY207-LEU259
AGLY282-LEU334

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsMOD_RES: N-acetylserine => ECO:0000269|Ref.7
ChainResidueDetails
ASER2

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: Phosphotyrosine; by SRC => ECO:0000269|PubMed:15302870, ECO:0000269|PubMed:28669632
ChainResidueDetails
ATYR24

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphoserine; by PKC => ECO:0000269|PubMed:28669632, ECO:0000269|PubMed:2946940
ChainResidueDetails
AGLU26

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: N6-acetyllysine; alternate => ECO:0000250|UniProtKB:P07356
ChainResidueDetails
ALYS49

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P07356
ChainResidueDetails
ALYS152
ALYS227

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER184

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P07356
ChainResidueDetails
ATYR199

site_idSWS_FT_FI8
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0007744|PubMed:28112733
ChainResidueDetails
ALYS49

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PDB entries from 2024-11-06

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