Structure of PDB 1ura Chain A

Receptor sequence
>1uraA (length=446) Species: 562 (Escherichia coli) [Search protein sequence]
MPVLENRAAQGDITAPGGARRLTGDQTAALRDSLSDKPAKNIILLIGNGM
GDSEITAARNYAEGAGGFFKGIDALPLTGQYTHYALNKKTGKPDYVTDSA
ASATAWSTGVKTYNGALGVDIHEKDHPTILEMAKAAGLATGNVSTAELQD
ATPAALVAHVTSRKCYGPSATSEKCPGNALEKGGKGSITEQLLNARADVT
LGGGAKTFAETATAGEWQGKTLREQAQARGYQLVSDAASLNSVTEANQQK
PLLGLFADGNMPVRWLGPKATYHGNIDKPAVTCTPNPQRNDSVPTLAQMT
DKAIELLSKNEKGFFLQVEGASIDKQDHAANPCGQIGETVDLDEAVQRAL
EFAKKEGNTLVIVTADHAHASQIVAPDTKAPGLTQALNTKDGAVMVMSYG
NSEEDSQEHTGSQLRIAAYGPHAANVVGLTDQTDLFYTMKAALGLK
3D structure
PDB1ura Kinetic and structural consequences of replacing the aspartate bridge by asparagine in the catalytic metal triad of Escherichia coli alkaline phosphatase.
ChainA
Resolution2.04 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) N51 S102 D153 T155 R166 E322 D327 K328 H331 D369 H370 H412
Catalytic site (residue number reindexed from 1) N48 S99 D150 T152 R163 E319 D324 K325 H328 D366 H367 H409
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 A D327 H331 H412 D324 H328 H409
BS02 ZN A N51 S102 D369 H370 N48 S99 D366 H367
BS03 PO4 A S102 R166 D327 H370 H412 S99 R163 D324 H367 H409
BS04 PO4 A R267 W268 R292 R264 W265 R289
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:1ura, PDBe:1ura, PDBj:1ura
PDBsum1ura
PubMed8648634
UniProtP00634|PPB_ECOLI Alkaline phosphatase (Gene Name=phoA)

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