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1W45

The 2.5 Angstroem structure of the K16A mutant of annexin A8, which has an intact N-terminus.

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
A0007599biological_processhemostasis
A0012506cellular_componentvesicle membrane
A0016197biological_processendosomal transport
A0019834molecular_functionphospholipase A2 inhibitor activity
A0031012cellular_componentextracellular matrix
A0031902cellular_componentlate endosome membrane
A0042383cellular_componentsarcolemma
A0043325molecular_functionphosphatidylinositol-3,4-bisphosphate binding
A0046872molecular_functionmetal ion binding
A0051015molecular_functionactin filament binding
B0001786molecular_functionphosphatidylserine binding
B0005509molecular_functioncalcium ion binding
B0005515molecular_functionprotein binding
B0005544molecular_functioncalcium-dependent phospholipid binding
B0005546molecular_functionphosphatidylinositol-4,5-bisphosphate binding
B0005547molecular_functionphosphatidylinositol-3,4,5-trisphosphate binding
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0005886cellular_componentplasma membrane
B0007032biological_processendosome organization
B0007596biological_processblood coagulation
B0007599biological_processhemostasis
B0012506cellular_componentvesicle membrane
B0016197biological_processendosomal transport
B0019834molecular_functionphospholipase A2 inhibitor activity
B0031012cellular_componentextracellular matrix
B0031902cellular_componentlate endosome membrane
B0042383cellular_componentsarcolemma
B0043325molecular_functionphosphatidylinositol-3,4-bisphosphate binding
B0046872molecular_functionmetal ion binding
B0051015molecular_functionactin filament binding
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 Residues142
DetailsRepeat: {"description":"Annexin 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU01245","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues142
DetailsRepeat: {"description":"Annexin 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU01245","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues144
DetailsRepeat: {"description":"Annexin 3","evidences":[{"source":"PROSITE-ProRule","id":"PRU01245","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues142
DetailsRepeat: {"description":"Annexin 4","evidences":[{"source":"PROSITE-ProRule","id":"PRU01245","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues8
DetailsBinding site: {}
ChainResidueDetails

247536

PDB entries from 2026-01-14

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