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2RAN

RAT ANNEXIN V CRYSTAL STRUCTURE: CA2+-INDUCED CONFORMATIONAL CHANGES

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
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA A 320
ChainResidue
AMET26
AGLY28
AGLY30
AGLU70
AHOH404

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CA A 321
ChainResidue
ALYS68
ALEU71
AGLU76
AHOH499

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE CA A 322
ChainResidue
ALEU98
AGLY100
AALA101
AGLY102
ATHR103
AASP142
AHOH408

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 323
ChainResidue
AVAL140
ATHR143
AGLN148
AHOH409
AHOH410
AHOH411

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 324
ChainResidue
AGLY181
ALYS184
AGLY186
AGLU226
AHOH412
AHOH414

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA A 325
ChainResidue
AASP224
ATHR227
AGLU232
AHOH418
AHOH503

site_idAC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 326
ChainResidue
AMET257
ALYS258
AALA260
AGLY261
AASP301
AHOH419

site_idAC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 327
ChainResidue
AARG23
ALYS27
AGLY28
AARG61

site_idAC9
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 328
ChainResidue
AARG283
ASER293
AGLY316
AGLU317

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

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsMOD_RES: N-acetylalanine => ECO:0000269|PubMed:7583670
ChainResidueDetails
ALEU3

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:22673903
ChainResidueDetails
AILE36

site_idSWS_FT_FI3
Number of Residues5
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P08758
ChainResidueDetails
ASER69
APHE75
ALEU78
AHIS96
AGLY100

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:P48036
ChainResidueDetails
AASN289

site_idSWS_FT_FI5
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0000250|UniProtKB:P08758
ChainResidueDetails
AGLY28

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PDB entries from 2024-07-17

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