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1HVD

STRUCTURAL AND ELECTROPHYSIOLOGICAL ANALYSIS OF ANNEXIN V MUTANTS. MUTAGENESIS OF HUMAN ANNEXIN V, AN IN VITRO VOLTAGE-GATED CALCIUM CHANNEL, PROVIDES INFORMATION ABOUT THE STRUCTURAL FEATURES OF THE ION PATHWAY, THE VOLTAGE SENSOR AND THE ION SELECTIVITY FILTER

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
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 600
ChainResidue
ALEU100
ALYS101
AGLY102
AGLY104
ATHR105
AASP144

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA A 601
ChainResidue
AASP303
AHOH483
AMET259
AGLY261
AGLY263

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA A 602
ChainResidue
AMET28
AGLY30
AGLY32
AGLU72
AHOH417

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CA A 603
ChainResidue
ATHR33
AGLU35
AHOH485

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 Residues1
DetailsMOD_RES: N-acetylalanine => ECO:0007744|PubMed:19413330
ChainResidueDetails
AGLN3

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P48036
ChainResidueDetails
AILE38

site_idSWS_FT_FI3
Number of Residues4
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861
ChainResidueDetails
ASER71
APHE77
ALEU80
AHIS98

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:16916647
ChainResidueDetails
AGLY102

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:P48036
ChainResidueDetails
AASN291

site_idSWS_FT_FI6
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0007744|PubMed:25772364, ECO:0007744|PubMed:28112733
ChainResidueDetails
AGLY30

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PDB entries from 2024-10-30

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