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1W3W

The 2.1 Angstroem resolution structure of annexin A8

Functional Information from GO Data
ChainGOidnamespacecontents
A0001786molecular_functionphosphatidylserine binding
A0005509molecular_functioncalcium ion binding
A0005515molecular_functionprotein binding
A0005544molecular_functioncalcium-dependent phospholipid binding
A0005546molecular_functionphosphatidylinositol-4,5-bisphosphate binding
A0005547molecular_functionphosphatidylinositol-3,4,5-trisphosphate binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0007032biological_processendosome organization
A0007596biological_processblood coagulation
A0012506cellular_componentvesicle membrane
A0016197biological_processendosomal transport
A0031902cellular_componentlate endosome membrane
A0042383cellular_componentsarcolemma
A0043325molecular_functionphosphatidylinositol-3,4-bisphosphate binding
A0046872molecular_functionmetal ion binding
A0051015molecular_functionactin filament binding
A0062023cellular_componentcollagen-containing extracellular matrix
A1900004biological_processnegative regulation of serine-type endopeptidase activity
A1900138biological_processnegative regulation of phospholipase A2 activity
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA A1328
ChainResidue
AMET266
AGLY268
AGLY270
AASP310
AHOH2086

Functional Information from PROSITE/UniProt
site_idPS00223
Number of Residues53
DetailsANNEXIN_1 Annexin repeat signature. GTneqaiidvLtkRsntQrqQiaksFkaqfgkdLtetLkselsGkferlIvaL
ChainResidueDetails
AGLY38-LEU90
AGLY110-LEU162
AGLY195-VAL247
AGLY270-LEU322

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsBINDING:
ChainResidueDetails
AMET266
AGLY268
AGLY270
AASP310

226707

PDB entries from 2024-10-30

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