Structure of PDB 5tpq Chain B

Receptor sequence
>5tpqB (length=444) Species: 83333 (Escherichia coli K-12) [Search protein sequence]
NRAAQGDITAPGGARRLTGDQTAALRDSLSDKPAKNIILLIGDGMGDSEI
TAARNYAEGAGGFFKGIDALPLTGQYTHYALNKKTGKPDYVTASAASATA
WSTGVKTYNGALGVDIHEKDHPTILEMAKAAGLATGNVSTAELQAATPAA
LVAHVTSSKCYGPSATSEKCPGNALEKGGKGSITEQLLNARADVTLGGGA
KTFAETATAGEWQGKTLREQAQARGYQLVSDAASLNSVTEANQQKPLLGL
FADGNMPVRWLGPKATYHGNIDKPAVTCTPNPQRNDSVPTLAQMTDKAIE
LLSKNEKGFFLQVAGASIDAQDHAANPCGQIGETVDLDEAVQRALEFAKK
EGNTLVIVTADHAHASQIVAPDTKAPGLTQALNTKDGAVMVMSYGNSEED
SQEHTGSQLRIAAYGPHAANVVGLTDQTDLFYTMKAALGLKWSH
3D structure
PDB5tpq Differential catalytic promiscuity of the alkaline phosphatase superfamily bimetallo core reveals mechanistic features underlying enzyme evolution.
ChainB
Resolution2.45 Å
3D
structure
Catalytic site residues are labeled in the structure
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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.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 ZN B D51 S102 D369 H370 D43 S94 D361 H362
BS02 ZN B D327 H331 H412 D319 H323 H404
BS03 ZN B E134 H162 H452 E126 H154 H444
BS04 PO4 B S102 D327 H412 S94 D319 H404
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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