Structure of PDB 5tpq Chain A Binding Site BS01

Receptor Information
>5tpq Chain A (length=446) Species: 83333 (Escherichia coli K-12) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
ENRAAQGDITAPGGARRLTGDQTAALRDSLSDKPAKNIILLIGDGMGDSE
ITAARNYAEGAGGFFKGIDALPLTGQYTHYALNKKTGKPDYVTASAASAT
AWSTGVKTYNGALGVDIHEKDHPTILEMAKAAGLATGNVSTAELQAATPA
ALVAHVTSSKCYGPSATSEKCPGNALEKGGKGSITEQLLNARADVTLGGG
AKTFAETATAGEWQGKTLREQAQARGYQLVSDAASLNSVTEANQQKPLLG
LFADGNMPVRWLGPKATYHGNIDKPAVTCTPNPQRNDSVPTLAQMTDKAI
ELLSKNEKGFFLQVAGASIDAQDHAANPCGQIGETVDLDEAVQRALEFAK
KEGNTLVIVTADHAHASQIVAPDTKAPGLTQALNTKDGAVMVMSYGNSEE
DSQEHTGSQLRIAAYGPHAANVVGLTDQTDLFYTMKAALGLKWSHP
Ligand information
Ligand IDZN
InChIInChI=1S/Zn/q+2
InChIKeyPTFCDOFLOPIGGS-UHFFFAOYSA-N
SMILES
SoftwareSMILES
CACTVS 3.341[Zn++]
ACDLabs 10.04
OpenEye OEToolkits 1.5.0		[Zn+2]
FormulaZn
NameZINC ION
ChEMBLCHEMBL1236970
DrugBankDB14532
ZINC
PDB chain5tpq Chain A Residue 501 [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)		D51 S102 D369 H370
Binding residue
(residue number reindexed from 1)		D44 S95 D362 H363
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) D44 S95 A146 T148 S159 A315 D320 A321 H324 D362 H363 H405
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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