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1ANX

THE CRYSTAL STRUCTURE OF A NEW HIGH-CALCIUM FORM OF ANNEXIN V

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
A0009897cellular_componentexternal side of plasma membrane
A0012506cellular_componentvesicle membrane
A0016020cellular_componentmembrane
A0042383cellular_componentsarcolemma
A0043066biological_processnegative regulation of apoptotic process
A0050819biological_processnegative regulation of coagulation
A0062023cellular_componentcollagen-containing extracellular matrix
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
B0009897cellular_componentexternal side of plasma membrane
B0012506cellular_componentvesicle membrane
B0016020cellular_componentmembrane
B0042383cellular_componentsarcolemma
B0043066biological_processnegative regulation of apoptotic process
B0050819biological_processnegative regulation of coagulation
B0062023cellular_componentcollagen-containing extracellular matrix
B0070062cellular_componentextracellular exosome
B0072563cellular_componentendothelial microparticle
C0001786molecular_functionphosphatidylserine binding
C0004859molecular_functionphospholipase inhibitor activity
C0005509molecular_functioncalcium ion binding
C0005515molecular_functionprotein binding
C0005543molecular_functionphospholipid binding
C0005544molecular_functioncalcium-dependent phospholipid binding
C0005576cellular_componentextracellular region
C0005737cellular_componentcytoplasm
C0005829cellular_componentcytosol
C0005925cellular_componentfocal adhesion
C0007165biological_processsignal transduction
C0007596biological_processblood coagulation
C0009897cellular_componentexternal side of plasma membrane
C0012506cellular_componentvesicle membrane
C0016020cellular_componentmembrane
C0042383cellular_componentsarcolemma
C0043066biological_processnegative regulation of apoptotic process
C0050819biological_processnegative regulation of coagulation
C0062023cellular_componentcollagen-containing extracellular matrix
C0070062cellular_componentextracellular exosome
C0072563cellular_componentendothelial microparticle
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 321
ChainResidue
AGLY183
ALYS186
AGLY188
AGLU228
ASO4322
AHOH326

site_idAC2
Number of Residues10
DetailsBINDING SITE FOR RESIDUE SO4 A 322
ChainResidue
ATHR189
AGLU228
ACA321
AHOH339
AHOH420
AHOH449
BGLN181
ALYS186
ATRP187
AGLY188

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CA A 323
ChainResidue
AMET28
AGLY30
AGLY32
AGLU72

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CA A 324
ChainResidue
ALYS70
ALEU73
AGLU78

site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CA A 325
ChainResidue
AASP226
ATHR229
AGLU234

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA B 321
ChainResidue
BGLY183
BLYS186
BGLY188
BGLU228
BSO4322
BHOH345

site_idAC7
Number of Residues9
DetailsBINDING SITE FOR RESIDUE SO4 B 322
ChainResidue
BLYS186
BGLY188
BTHR189
BGLU228
BCA321
BHOH345
BHOH362
BHOH382
CGLN181

site_idAC8
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA B 323
ChainResidue
BMET28
BGLY30
BGLY32
BGLU72
BHOH441

site_idAC9
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CA B 324
ChainResidue
BLYS70
BLEU73
BGLU78
BHOH455

site_idBC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CA B 325
ChainResidue
BASP226
BTHR229
BGLU234

site_idBC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA C 321
ChainResidue
CGLY183
CLYS186
CGLY188
CGLU228
CSO4322
CHOH333

site_idBC3
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SO4 C 322
ChainResidue
AGLN181
CLYS186
CTRP187
CGLY188
CTHR189
CGLU228
CCA321
CHOH441

site_idBC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA C 323
ChainResidue
CMET28
CGLY30
CGLY32
CGLU72
CHOH385

site_idBC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CA C 324
ChainResidue
CLYS70
CLEU73
CGLU78

site_idBC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CA C 325
ChainResidue
CASP226
CTHR229
CGLU234

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 Residues3
DetailsMOD_RES: N-acetylalanine => ECO:0007744|PubMed:19413330
ChainResidueDetails
AGLN3
BGLN3
CGLN3

site_idSWS_FT_FI2
Number of Residues3
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P48036
ChainResidueDetails
AILE38
BILE38
CILE38

site_idSWS_FT_FI3
Number of Residues12
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861
ChainResidueDetails
ASER71
CPHE77
CLEU80
CHIS98
APHE77
ALEU80
AHIS98
BSER71
BPHE77
BLEU80
BHIS98
CSER71

site_idSWS_FT_FI4
Number of Residues3
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:16916647
ChainResidueDetails
AGLY102
BGLY102
CGLY102

site_idSWS_FT_FI5
Number of Residues3
DetailsMOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:P48036
ChainResidueDetails
AASN291
BASN291
CASN291

site_idSWS_FT_FI6
Number of Residues6
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0007744|PubMed:25772364, ECO:0007744|PubMed:28112733
ChainResidueDetails
AGLY30
BGLY30
CGLY30

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PDB entries from 2024-10-30

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