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2H0K

Crystal Structure of a Mutant of Rat Annexin A5

Functional Information from GO Data
ChainGOidnamespacecontents
A0001786molecular_functionphosphatidylserine binding
A0005388molecular_functionP-type calcium transporter activity
A0005509molecular_functioncalcium ion binding
A0005515molecular_functionprotein binding
A0005543molecular_functionphospholipid binding
A0005544molecular_functioncalcium-dependent phospholipid binding
A0005615cellular_componentextracellular space
A0005737cellular_componentcytoplasm
A0007596biological_processblood coagulation
A0008021cellular_componentsynaptic vesicle
A0009897cellular_componentexternal side of plasma membrane
A0012506cellular_componentvesicle membrane
A0014704cellular_componentintercalated disc
A0017046molecular_functionpeptide hormone binding
A0030018cellular_componentZ disc
A0030195biological_processnegative regulation of blood coagulation
A0030425cellular_componentdendrite
A0030672cellular_componentsynaptic vesicle membrane
A0030971molecular_functionreceptor tyrosine kinase binding
A0042383cellular_componentsarcolemma
A0042802molecular_functionidentical protein binding
A0042995cellular_componentcell projection
A0043025cellular_componentneuronal cell body
A0043065biological_processpositive regulation of apoptotic process
A0043204cellular_componentperikaryon
A0043679cellular_componentaxon terminus
A0050819biological_processnegative regulation of coagulation
A0051592biological_processresponse to calcium ion
A0070588biological_processcalcium ion transmembrane transport
A0071284biological_processcellular response to lead ion
A0072563cellular_componentendothelial microparticle
A0097066biological_processresponse to thyroid hormone
A0097211biological_processcellular response to gonadotropin-releasing hormone
A1901317biological_processregulation of flagellated sperm motility
A1902721biological_processnegative regulation of prolactin secretion
B0001786molecular_functionphosphatidylserine binding
B0005388molecular_functionP-type calcium transporter activity
B0005509molecular_functioncalcium ion binding
B0005515molecular_functionprotein binding
B0005543molecular_functionphospholipid binding
B0005544molecular_functioncalcium-dependent phospholipid binding
B0005615cellular_componentextracellular space
B0005737cellular_componentcytoplasm
B0007596biological_processblood coagulation
B0008021cellular_componentsynaptic vesicle
B0009897cellular_componentexternal side of plasma membrane
B0012506cellular_componentvesicle membrane
B0014704cellular_componentintercalated disc
B0017046molecular_functionpeptide hormone binding
B0030018cellular_componentZ disc
B0030195biological_processnegative regulation of blood coagulation
B0030425cellular_componentdendrite
B0030672cellular_componentsynaptic vesicle membrane
B0030971molecular_functionreceptor tyrosine kinase binding
B0042383cellular_componentsarcolemma
B0042802molecular_functionidentical protein binding
B0042995cellular_componentcell projection
B0043025cellular_componentneuronal cell body
B0043065biological_processpositive regulation of apoptotic process
B0043204cellular_componentperikaryon
B0043679cellular_componentaxon terminus
B0050819biological_processnegative regulation of coagulation
B0051592biological_processresponse to calcium ion
B0070588biological_processcalcium ion transmembrane transport
B0071284biological_processcellular response to lead ion
B0072563cellular_componentendothelial microparticle
B0097066biological_processresponse to thyroid hormone
B0097211biological_processcellular response to gonadotropin-releasing hormone
B1901317biological_processregulation of flagellated sperm motility
B1902721biological_processnegative regulation of prolactin secretion
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CA A 401
ChainResidue
AMET26
AGLY28
AGLY30
AGLU70

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CA A 402
ChainResidue
ALYS68
ALEU71
AGLU76
AHOH477

site_idAC3
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CA A 403
ChainResidue
AGLU33
ATHR31

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA A 404
ChainResidue
ALEU98
AGLY100
AALA101
ATHR103
AASP142

site_idAC5
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CA A 412
ChainResidue
ATHR187
AGLU226

site_idAC6
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CA A 406
ChainResidue
ATHR103
AGLU105

site_idAC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CA B 402
ChainResidue
BLYS68
BLEU71
BGLU76
BHOH451

site_idAC8
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CA B 403
ChainResidue
AASP34
BTHR31
BGLU33

site_idAC9
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA B 404
ChainResidue
BLEU98
BGLY100
BALA101
BTHR103
BASP142

site_idBC1
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CA B 412
ChainResidue
BTHR187
BGLU226

site_idBC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CA B 406
ChainResidue
BTHR103
BGLU105

site_idBC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CA A 409
ChainResidue
ATHR187
AGLU189
AHOH415

site_idBC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA A 410
ChainResidue
AMET257
AGLY259
AGLY261
AASP301
AHOH416

site_idBC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CA A 408
ChainResidue
AASP224
ATHR227
AGLU232
AHOH417

site_idBC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA A 407
ChainResidue
AGLY181
ALYS184
AGLY186
AGLU226
AHOH418

site_idBC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CA A 414
ChainResidue
AGLU93
AHIS96
AHIS265
AHOH419

site_idBC8
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA B 401
ChainResidue
BMET26
BGLY28
BGLY30
BGLU70
BHOH415

site_idBC9
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CA B 409
ChainResidue
BTHR187
BGLU189
BHOH416

site_idCC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA B 410
ChainResidue
BMET257
BGLY259
BGLY261
BASP301
BHOH417
BHOH464

site_idCC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CA B 408
ChainResidue
BASP224
BTHR227
BGLU232
BHOH418

site_idCC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA B 407
ChainResidue
BGLY181
BLYS184
BGLY186
BGLU226
BHOH419

site_idCC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CA B 414
ChainResidue
BGLU93
BHIS96
BHIS265
BHOH420

Functional Information from PROSITE/UniProt
site_idPS00223
Number of Residues53
DetailsANNEXIN_1 Annexin repeat signature. GTdedsilnlLtaRsnaQrqQiaeeFetlfgrdLvndMkseltGkfeklIvaL
ChainResidueDetails
AGLY30-LEU82
AGLY102-LEU154
AGLY186-VAL238
AGLY261-LEU313

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsMOD_RES: N-acetylalanine => ECO:0000269|PubMed:7583670
ChainResidueDetails
ALEU3
BLEU3

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:22673903
ChainResidueDetails
AILE36
BILE36

site_idSWS_FT_FI3
Number of Residues10
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P08758
ChainResidueDetails
ASER69
BGLY100
APHE75
ALEU78
AHIS96
AGLY100
BSER69
BPHE75
BLEU78
BHIS96

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:P48036
ChainResidueDetails
AASN289
BASN289

site_idSWS_FT_FI5
Number of Residues4
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0000250|UniProtKB:P08758
ChainResidueDetails
AGLY28
BGLY28

223166

PDB entries from 2024-07-31

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