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1AVH

CRYSTAL AND MOLECULAR STRUCTURE OF HUMAN ANNEXIN V AFTER REFINEMENT. IMPLICATIONS FOR STRUCTURE, MEMBRANE BINDING AND ION CHANNEL FORMATION OF THE ANNEXIN FAMILY OF PROTEINS

Functional Information from GO Data
ChainGOidnamespacecontents
A0001786molecular_functionphosphatidylserine binding
A0004859molecular_functionphospholipase inhibitor activity
A0005509molecular_functioncalcium ion binding
A0005515molecular_functionprotein binding
A0005543molecular_functionphospholipid binding
A0005544molecular_functioncalcium-dependent phospholipid binding
A0005576cellular_componentextracellular region
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0005925cellular_componentfocal adhesion
A0007165biological_processsignal transduction
A0007596biological_processblood coagulation
A0007599biological_processhemostasis
A0009897cellular_componentexternal side of plasma membrane
A0012506cellular_componentvesicle membrane
A0016020cellular_componentmembrane
A0031012cellular_componentextracellular matrix
A0042383cellular_componentsarcolemma
A0043066biological_processnegative regulation of apoptotic process
A0050819biological_processnegative regulation of coagulation
A0070062cellular_componentextracellular exosome
A0072563cellular_componentendothelial microparticle
B0001786molecular_functionphosphatidylserine binding
B0004859molecular_functionphospholipase inhibitor activity
B0005509molecular_functioncalcium ion binding
B0005515molecular_functionprotein binding
B0005543molecular_functionphospholipid binding
B0005544molecular_functioncalcium-dependent phospholipid binding
B0005576cellular_componentextracellular region
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0005925cellular_componentfocal adhesion
B0007165biological_processsignal transduction
B0007596biological_processblood coagulation
B0007599biological_processhemostasis
B0009897cellular_componentexternal side of plasma membrane
B0012506cellular_componentvesicle membrane
B0016020cellular_componentmembrane
B0031012cellular_componentextracellular matrix
B0042383cellular_componentsarcolemma
B0043066biological_processnegative regulation of apoptotic process
B0050819biological_processnegative regulation of coagulation
B0070062cellular_componentextracellular exosome
B0072563cellular_componentendothelial microparticle
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CA A 321
ChainResidue
ALEU100
AGLY102
AGLY104
BLEU31

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA B 321
ChainResidue
BMET28
BGLY30
BGLY32
BTHR33
BGLU72

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CA B 322
ChainResidue
BMET259
BGLY261
BGLY263
BASP303

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 541
ChainResidue
ALYS79
AHOH676
BALA262
BGLY263
BTHR264
BHOH787

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 543
ChainResidue
AGLY75
ALYS76
AHOH656
AHOH819

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 B 542
ChainResidue
ATHR105
BARG25
BGLY30
BARG63

site_idAC7
Number of Residues2
DetailsBINDING SITE FOR RESIDUE SO4 B 545
ChainResidue
BGLU22
BARG201

Functional Information from PROSITE/UniProt
site_idPS00223
Number of Residues53
DetailsANNEXIN_1 Annexin repeat signature. GTdeesiltlLtsRsnaQrqEisaaFktlfgrdLlddLkseltGkfeklIvaL
ChainResidueDetails
AGLY32-LEU84
AGLY104-LEU156
AGLY188-VAL240
AGLY263-LEU315

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 Residues10
DetailsMotif: {"description":"[IL]-x-C-x-x-[DE] motif","evidences":[{"source":"PubMed","id":"25417112","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P48036","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues8
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues2
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"16916647","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues2
DetailsModified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"P48036","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues4
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate","evidences":[{"source":"PubMed","id":"25772364","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"28112733","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

239149

PDB entries from 2025-07-23

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