Structure of PDB 5tpq Chain B Binding Site BS04

Receptor Information
>5tpq Chain B (length=444) Species: 83333 (Escherichia coli K-12) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
NRAAQGDITAPGGARRLTGDQTAALRDSLSDKPAKNIILLIGDGMGDSEI
TAARNYAEGAGGFFKGIDALPLTGQYTHYALNKKTGKPDYVTASAASATA
WSTGVKTYNGALGVDIHEKDHPTILEMAKAAGLATGNVSTAELQAATPAA
LVAHVTSSKCYGPSATSEKCPGNALEKGGKGSITEQLLNARADVTLGGGA
KTFAETATAGEWQGKTLREQAQARGYQLVSDAASLNSVTEANQQKPLLGL
FADGNMPVRWLGPKATYHGNIDKPAVTCTPNPQRNDSVPTLAQMTDKAIE
LLSKNEKGFFLQVAGASIDAQDHAANPCGQIGETVDLDEAVQRALEFAKK
EGNTLVIVTADHAHASQIVAPDTKAPGLTQALNTKDGAVMVMSYGNSEED
SQEHTGSQLRIAAYGPHAANVVGLTDQTDLFYTMKAALGLKWSH
Ligand information
Ligand IDPO4
InChIInChI=1S/H3O4P/c1-5(2,3)4/h(H3,1,2,3,4)/p-3
InChIKeyNBIIXXVUZAFLBC-UHFFFAOYSA-K
SMILES
SoftwareSMILES
CACTVS 3.341[O-][P]([O-])([O-])=O
ACDLabs 10.04[O-]P([O-])([O-])=O
OpenEye OEToolkits 1.5.0[O-]P(=O)([O-])[O-]
FormulaO4 P
NamePHOSPHATE ION
ChEMBL
DrugBankDB14523
ZINC
PDB chain5tpq Chain B Residue 504 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB5tpq Differential catalytic promiscuity of the alkaline phosphatase superfamily bimetallo core reveals mechanistic features underlying enzyme evolution.
Resolution2.45 Å
Binding residue
(original residue number in PDB)		S102 D327 H412
Binding residue
(residue number reindexed from 1)		S94 D319 H404
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) D51 S102 A153 T155 S166 A322 D327 A328 H331 D369 H370 H412
Catalytic site (residue number reindexed from 1) D43 S94 A145 T147 S158 A314 D319 A320 H323 D361 H362 H404
Enzyme Commision number 3.1.3.1: alkaline phosphatase.
Gene Ontology
Molecular Function
GO:0000287 magnesium ion binding
GO:0004035 alkaline phosphatase activity
GO:0004721 phosphoprotein phosphatase activity
GO:0005515 protein binding
GO:0008270 zinc ion binding
GO:0016787 hydrolase activity
GO:0016791 phosphatase activity
GO:0030613 oxidoreductase activity, acting on phosphorus or arsenic in donors
GO:0033748 hydrogenase (acceptor) activity
GO:0046872 metal ion binding
Biological Process
GO:0006470 protein dephosphorylation
Cellular Component
GO:0030288 outer membrane-bounded periplasmic space
GO:0042597 periplasmic space

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:5tpq, PDBe:5tpq, PDBj:5tpq
PDBsum5tpq
PubMed29070681
UniProtP00634|PPB_ECOLI Alkaline phosphatase (Gene Name=phoA)

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