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1AVC

BOVINE ANNEXIN VI (CALCIUM-BOUND)

Functional Information from GO Data
ChainGOidnamespacecontents
A0001725cellular_componentstress fiber
A0001755biological_processneural crest cell migration
A0001778biological_processplasma membrane repair
A0001786molecular_functionphosphatidylserine binding
A0003418biological_processgrowth plate cartilage chondrocyte differentiation
A0005262molecular_functioncalcium channel activity
A0005509molecular_functioncalcium ion binding
A0005525molecular_functionGTP binding
A0005544molecular_functioncalcium-dependent phospholipid binding
A0005737cellular_componentcytoplasm
A0005886cellular_componentplasma membrane
A0005925cellular_componentfocal adhesion
A0006816biological_processcalcium ion transport
A0006937biological_processregulation of muscle contraction
A0008201molecular_functionheparin binding
A0015276molecular_functionligand-gated monoatomic ion channel activity
A0015485molecular_functioncholesterol binding
A0016020cellular_componentmembrane
A0016192biological_processvesicle-mediated transport
A0019899molecular_functionenzyme binding
A0030061cellular_componentmitochondrial crista
A0031214biological_processbiomineral tissue development
A0031982cellular_componentvesicle
A0035374molecular_functionchondroitin sulfate binding
A0038024molecular_functioncargo receptor activity
A0042383cellular_componentsarcolemma
A0042470cellular_componentmelanosome
A0042584cellular_componentchromaffin granule membrane
A0048306molecular_functioncalcium-dependent protein binding
A0048471cellular_componentperinuclear region of cytoplasm
A0051015molecular_functionactin filament binding
A0051283biological_processnegative regulation of sequestering of calcium ion
A0051560biological_processmitochondrial calcium ion homeostasis
A0070509biological_processcalcium ion import
A0070588biological_processcalcium ion transmembrane transport
A0097190biological_processapoptotic signaling pathway
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 674
ChainResidue
AMET376
AGLY378
ALEU379
AGLY380
ATHR381
AGLU420

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CA A 675
ChainResidue
AGLU83
ALYS75
ALEU78
ATHR79

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 676
ChainResidue
AMET264
AGLY266
ALEU267
AGLY268
ATHR269
AASP308

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE CA A 677
ChainResidue
AGLY188
AGLU189
ALYS191
AGLY193
ATHR194
ASER229
AGLU233

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 678
ChainResidue
AMET612
AGLY614
AALA615
AGLY616
ATHR617
AASP656

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA A 679
ChainResidue
AMET448
AGLU449
AGLY450
AGLY452
AASP492

Functional Information from PROSITE/UniProt
site_idPS00223
Number of Residues53
DetailsANNEXIN_1 Annexin repeat signature. GSdkeaiinlItsRsnkQrqEicqnYkslygkdLiadLkyeltGkferlIvgL
ChainResidueDetails
AGLY37-LEU89
AGLY109-LEU161
AGLY193-VAL245
AGLY268-LEU320
AGLY380-LEU432
AGLY452-LEU504
AGLY616-ILE668

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsMOD_RES: N-acetylalanine => ECO:0000250|UniProtKB:P08133
ChainResidueDetails
AGLU57

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P08133
ChainResidueDetails
ALYS68
AALA592

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P08133
ChainResidueDetails
ALEU85

site_idSWS_FT_FI4
Number of Residues9
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P08133
ChainResidueDetails
AILE118
ATHR123
ALEU130
AASP136
AGLY361
ALEU425
AILE473
AGLY538
ALYS620

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P14824
ChainResidueDetails
APHE256

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P48037
ChainResidueDetails
ATYR477

218853

PDB entries from 2024-04-24

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