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1AXN

THE HIGH RESOLUTION STRUCTURE OF ANNEXIN III SHOWS DIFFERENCES WITH ANNEXIN V

Functional Information from GO Data
ChainGOidnamespacecontents
A0001786molecular_functionphosphatidylserine binding
A0004859molecular_functionphospholipase inhibitor activity
A0005509molecular_functioncalcium ion binding
A0005544molecular_functioncalcium-dependent phospholipid binding
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005886cellular_componentplasma membrane
A0006909biological_processphagocytosis
A0010595biological_processpositive regulation of endothelial cell migration
A0012506cellular_componentvesicle membrane
A0016020cellular_componentmembrane
A0019834molecular_functionphospholipase A2 inhibitor activity
A0030670cellular_componentphagocytic vesicle membrane
A0042581cellular_componentspecific granule
A0042742biological_processdefense response to bacterium
A0043312biological_processneutrophil degranulation
A0045766biological_processpositive regulation of angiogenesis
A0048306molecular_functioncalcium-dependent protein binding
A0051091biological_processpositive regulation of DNA-binding transcription factor activity
A0070062cellular_componentextracellular exosome
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA A 351
ChainResidue
AILE32
AGLY34
AGLY36
ATHR37
AASP76

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA A 352
ChainResidue
AGLU148
AMET104
AGLY106
AGLY108
ATHR109

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 353
ChainResidue
AGLY187
AARG190
AGLY192
AGLU232
AHOH406
AHOH407

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CA A 354
ChainResidue
ALYS230
ALEU233
AGLU238
AHOH580

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CA A 355
ChainResidue
ATHR193
AGLU195
AHOH458
AHOH603

Functional Information from PROSITE/UniProt
site_idPS00223
Number of Residues53
DetailsANNEXIN_1 Annexin repeat signature. GTdekmlisiLteRsnaQrqLivkeYqaaygkeLkddLkgdlsGhfehlMvaL
ChainResidueDetails
AGLY36-LEU88
AGLY108-LEU160
AGLY192-ILE244
AGLY267-ILE319

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsMOD_RES: N-acetylalanine => ECO:0000269|Ref.9
ChainResidueDetails
AALA3

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P14669
ChainResidueDetails
ATHR268

237735

PDB entries from 2025-06-18

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