Structure of PDB 7yiv Chain E Binding Site BS03

Receptor Information
>7yiv Chain E (length=484) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
LVPEKEKDPKYWRDQAQETLKYALELQKLNTNVAKNVIMFLGDGMGVSTV
TAARILKGQLHHNPGEETRLEMDKFPFVALSKTYNTNAQVPDSAGTATAY
LCGVKANEGTVGVSAATERSRCNTTQGNEVTSILRWAKDAGKSVGIVTTT
RVNHATPSAAYAHSADRDWYSDNEMPPEALSQGCKDIAYQLMHNIRDIDV
IMGGGRKYMYPKNKTDVEYESDEKARGTRLDGLDLVDTWKSFKPRYKHSH
FIWNRTELLTLDPHNVDYLLGLFEPGDMQYELNRNNVTDPSLSEMVVVAI
QILRKNPKGFFLLVEGGRIDHGHHEGKAKQALHEAVEMDRAIGQAGSLTS
SEDTLTVVTADHSHVFTFGGYTPRGNSIFGLAPMLSDTDKKPFTAILYGN
GPGYKVVGGERENVSMVDYAHNNYQAQSAVPLRHETHGGEDVAVFSKGPM
AHLLHGVHEQNYVPHVMAYAACIGANLGHCAPAA
Ligand information
Ligand IDCA
InChIInChI=1S/Ca/q+2
InChIKeyBHPQYMZQTOCNFJ-UHFFFAOYSA-N
SMILES
SoftwareSMILES
CACTVS 3.341[Ca++]
ACDLabs 10.04
OpenEye OEToolkits 1.5.0		[Ca+2]
FormulaCa
NameCALCIUM ION
ChEMBL
DrugBankDB14577
ZINC
PDB chain7yiv Chain E Residue 605 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
PDB7yiv The structural pathology for hypophosphatasia caused by malfunctional tissue non-specific alkaline phosphatase.
Resolution3.18 Å
Binding residue
(original residue number in PDB)		E235 F290 E291 D306
Binding residue
(residue number reindexed from 1)		E218 F273 E274 D289
Annotation score1
Enzymatic activity
Enzyme Commision number 3.1.3.1: alkaline phosphatase.
3.9.1.1: phosphoamidase.
Gene Ontology
Molecular Function
GO:0004035 alkaline phosphatase activity
GO:0004427 inorganic diphosphate phosphatase activity
GO:0005509 calcium ion binding
GO:0016462 pyrophosphatase activity
GO:0016787 hydrolase activity
GO:0016791 phosphatase activity
GO:0016887 ATP hydrolysis activity
GO:0033883 pyridoxal phosphatase activity
GO:0043262 ADP phosphatase activity
GO:0046872 metal ion binding
GO:0050187 phosphoamidase activity
GO:0052732 phosphoethanolamine phosphatase activity
Biological Process
GO:0001501 skeletal system development
GO:0001649 osteoblast differentiation
GO:0001958 endochondral ossification
GO:0003006 developmental process involved in reproduction
GO:0014070 response to organic cyclic compound
GO:0019725 cellular homeostasis
GO:0030282 bone mineralization
GO:0031214 biomineral tissue development
GO:0032496 response to lipopolysaccharide
GO:0032868 response to insulin
GO:0033280 response to vitamin D
GO:0034516 response to vitamin B6
GO:0036005 response to macrophage colony-stimulating factor
GO:0042822 pyridoxal phosphate metabolic process
GO:0046677 response to antibiotic
GO:0051384 response to glucocorticoid
GO:0055062 phosphate ion homeostasis
GO:0055074 calcium ion homeostasis
GO:0071407 cellular response to organic cyclic compound
GO:0071529 cementum mineralization
GO:0120162 positive regulation of cold-induced thermogenesis
GO:0140651 futile creatine cycle
GO:0140928 inhibition of non-skeletal tissue mineralization
GO:1904383 response to sodium phosphate
Cellular Component
GO:0005576 extracellular region
GO:0005615 extracellular space
GO:0005739 mitochondrion
GO:0005758 mitochondrial intermembrane space
GO:0005886 plasma membrane
GO:0016020 membrane
GO:0031012 extracellular matrix
GO:0031966 mitochondrial membrane
GO:0065010 extracellular membrane-bounded organelle
GO:0070062 extracellular exosome
GO:0098552 side of membrane

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:7yiv, PDBe:7yiv, PDBj:7yiv
PDBsum7yiv
PubMed37422472
UniProtP05186|PPBT_HUMAN Alkaline phosphatase, tissue-nonspecific isozyme (Gene Name=ALPL)

[Back to BioLiP]