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4X9P

Crystal structure of bovine Annexin A2

Functional Information from GO Data
ChainGOidnamespacecontents
A0001786molecular_functionphosphatidylserine binding
A0002020molecular_functionprotease binding
A0004859molecular_functionphospholipase inhibitor activity
A0005262molecular_functioncalcium channel 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
A0005768cellular_componentendosome
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0008092molecular_functioncytoskeletal protein binding
A0016020cellular_componentmembrane
A0019834molecular_functionphospholipase A2 inhibitor activity
A0031214biological_processbiomineral tissue development
A0031982cellular_componentvesicle
A0042470cellular_componentmelanosome
A0043231cellular_componentintracellular membrane-bounded organelle
A0046790molecular_functionvirion binding
A0062023cellular_componentcollagen-containing extracellular matrix
A0065010cellular_componentextracellular membrane-bounded organelle
A0070509biological_processcalcium ion import
A0070588biological_processcalcium ion transmembrane transport
A0098641molecular_functioncadherin binding involved in cell-cell adhesion
A1905602biological_processpositive regulation of receptor-mediated endocytosis involved in cholesterol transport
Functional Information from PDB Data
site_idAC1
Number of Residues6
Detailsbinding site for residue CA A 401
ChainResidue
ASER234
AMET278
AGLY280
AGLY282
AASP322
AHOH567

site_idAC2
Number of Residues6
Detailsbinding site for residue CA A 402
ChainResidue
AGLY207
AGLU247
AHOH749
AGLY202
AARG205
ALYS206

site_idAC3
Number of Residues3
Detailsbinding site for residue CA A 403
ChainResidue
AGLY50
AVAL51
AGLU53

site_idAC4
Number of Residues2
Detailsbinding site for residue CL A 404
ChainResidue
AHIS94
AARG178

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|PubMed:2942542
ChainResidueDetails
ASER2

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: Phosphotyrosine; by SRC => ECO:0000250|UniProtKB:P07355
ChainResidueDetails
ATYR24

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphoserine; by PKC => ECO:0000250|UniProtKB:P07355
ChainResidueDetails
ASER26

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:0000250|UniProtKB:P07355
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:0000250|UniProtKB:P07355
ChainResidueDetails
ALYS49

218853

PDB entries from 2024-04-24

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