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7YIX

The Cryo-EM Structure of Human Tissue Nonspecific Alkaline Phosphatase and Single-Chain Fragment Variable (ScFv) Complex.

Functional Information from GO Data
ChainGOidnamespacecontents
A0001501biological_processskeletal system development
A0001649biological_processosteoblast differentiation
A0001958biological_processendochondral ossification
A0003006biological_processdevelopmental process involved in reproduction
A0004035molecular_functionalkaline phosphatase activity
A0004427molecular_functioninorganic diphosphate phosphatase activity
A0005509molecular_functioncalcium ion binding
A0005576cellular_componentextracellular region
A0005615cellular_componentextracellular space
A0005739cellular_componentmitochondrion
A0005758cellular_componentmitochondrial intermembrane space
A0005886cellular_componentplasma membrane
A0014070biological_processresponse to organic cyclic compound
A0016020cellular_componentmembrane
A0016462molecular_functionpyrophosphatase activity
A0016787molecular_functionhydrolase activity
A0016791molecular_functionphosphatase activity
A0016887molecular_functionATP hydrolysis activity
A0019725biological_processcellular homeostasis
A0030282biological_processbone mineralization
A0031012cellular_componentextracellular matrix
A0031214biological_processbiomineral tissue development
A0031966cellular_componentmitochondrial membrane
A0032496biological_processresponse to lipopolysaccharide
A0032868biological_processresponse to insulin
A0033280biological_processresponse to vitamin D
A0033883molecular_functionpyridoxal phosphatase activity
A0034516biological_processresponse to vitamin B6
A0036005biological_processresponse to macrophage colony-stimulating factor
A0042822biological_processpyridoxal phosphate metabolic process
A0043262molecular_functionADP phosphatase activity
A0046677biological_processresponse to antibiotic
A0046872molecular_functionmetal ion binding
A0050187molecular_functionphosphoamidase activity
A0051384biological_processresponse to glucocorticoid
A0052732molecular_functionphosphoethanolamine phosphatase activity
A0055062biological_processphosphate ion homeostasis
A0055074biological_processcalcium ion homeostasis
A0065010cellular_componentextracellular membrane-bounded organelle
A0070062cellular_componentextracellular exosome
A0071407biological_processcellular response to organic cyclic compound
A0071529biological_processcementum mineralization
A0098552cellular_componentside of membrane
A0120162biological_processpositive regulation of cold-induced thermogenesis
A0140651biological_processfutile creatine cycle
A0140928biological_processinhibition of non-skeletal tissue mineralization
A1904383biological_processresponse to sodium phosphate
B0001501biological_processskeletal system development
B0001649biological_processosteoblast differentiation
B0001958biological_processendochondral ossification
B0003006biological_processdevelopmental process involved in reproduction
B0004035molecular_functionalkaline phosphatase activity
B0004427molecular_functioninorganic diphosphate phosphatase activity
B0005509molecular_functioncalcium ion binding
B0005576cellular_componentextracellular region
B0005615cellular_componentextracellular space
B0005739cellular_componentmitochondrion
B0005758cellular_componentmitochondrial intermembrane space
B0005886cellular_componentplasma membrane
B0014070biological_processresponse to organic cyclic compound
B0016020cellular_componentmembrane
B0016462molecular_functionpyrophosphatase activity
B0016787molecular_functionhydrolase activity
B0016791molecular_functionphosphatase activity
B0016887molecular_functionATP hydrolysis activity
B0019725biological_processcellular homeostasis
B0030282biological_processbone mineralization
B0031012cellular_componentextracellular matrix
B0031214biological_processbiomineral tissue development
B0031966cellular_componentmitochondrial membrane
B0032496biological_processresponse to lipopolysaccharide
B0032868biological_processresponse to insulin
B0033280biological_processresponse to vitamin D
B0033883molecular_functionpyridoxal phosphatase activity
B0034516biological_processresponse to vitamin B6
B0036005biological_processresponse to macrophage colony-stimulating factor
B0042822biological_processpyridoxal phosphate metabolic process
B0043262molecular_functionADP phosphatase activity
B0046677biological_processresponse to antibiotic
B0046872molecular_functionmetal ion binding
B0050187molecular_functionphosphoamidase activity
B0051384biological_processresponse to glucocorticoid
B0052732molecular_functionphosphoethanolamine phosphatase activity
B0055062biological_processphosphate ion homeostasis
B0055074biological_processcalcium ion homeostasis
B0065010cellular_componentextracellular membrane-bounded organelle
B0070062cellular_componentextracellular exosome
B0071407biological_processcellular response to organic cyclic compound
B0071529biological_processcementum mineralization
B0098552cellular_componentside of membrane
B0120162biological_processpositive regulation of cold-induced thermogenesis
B0140651biological_processfutile creatine cycle
B0140928biological_processinhibition of non-skeletal tissue mineralization
B1904383biological_processresponse to sodium phosphate
Functional Information from PROSITE/UniProt
site_idPS00123
Number of Residues9
DetailsALKALINE_PHOSPHATASE Alkaline phosphatase active site. VpDSAGTAT
ChainResidueDetails
AVAL107-THR115

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Phosphoserine intermediate => ECO:0000250|UniProtKB:P05187, ECO:0000255|PROSITE-ProRule:PRU10042
ChainResidueDetails
ASER110
BSER110

site_idSWS_FT_FI2
Number of Residues18
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P05187
ChainResidueDetails
AASP60
BASP60
BSER110
BTHR173
BGLU332
BASP337
BHIS341
BASP378
BHIS379
BHIS454
ASER110
ATHR173
AGLU332
AASP337
AHIS341
AASP378
AHIS379
AHIS454

site_idSWS_FT_FI3
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:11395499
ChainResidueDetails
AGLU235
APHE290
AGLU291
AASP306
BGLU235
BPHE290
BGLU291
BASP306

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P09242
ChainResidueDetails
ASER110
BSER110

site_idSWS_FT_FI5
Number of Residues8
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASN140
AASN230
AASN271
AASN303
BASN140
BASN230
BASN271
BASN303

site_idSWS_FT_FI6
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19159218
ChainResidueDetails
AASN430
BASN430

222624

PDB entries from 2024-07-17

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