Structure of PDB 2anh Chain A

Receptor sequence
>2anhA (length=446) Species: 562 (Escherichia coli) [Search protein sequence]
MPVLENRAAQGDITAPGGARRLTGDQTAALRDSLSDKPAKNIILLIGDGM
GDSEITAARNYAEGAGGFFKGIDALPLTGQYTHYALNKKTGKPDYVTDSA
ASATAWSTGVKTYNGALGVDIHEKDHPTILEMAKAAGLATGNVSTAELQH
ATPAALVAHVTSRKCYGPSATSEKCPGNALEKGGKGSITEQLLNARADVT
LGGGAKTFAETATAGEWQGKTLREQAQARGYQLVSDAASLNSVTEANQQK
PLLGLFADGNMPVRWLGPKATYHGNIDKPAVTCTPNPQRNDSVPTLAQMT
DKAIELLSKNEKGFFLQVEGASIDKQDHAANPCGQIGETVDLDEAVQRAL
EFAKKEGNTLVIVTADHAHASQIVAPDTKAPGLTQALNTKDGAVMVMSYG
NSEEDSQEHTGSQLRIAAYGPHAANVVGLTDQTDLFYTMKAALGLK
3D structure
PDB2anh Mutations at positions 153 and 328 in Escherichia coli alkaline phosphatase provide insight towards the structure and function of mammalian and yeast alkaline phosphatases.
ChainA
Resolution2.4 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 H153 T155 R166 E322 D327 K328 H331 D369 H370 H412
Catalytic site (residue number reindexed from 1) D48 S99 H150 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 D51 S102 D369 H370 D48 S99 D366 H367
BS03 ZN A D51 H153 T155 E322 D48 H150 T152 E319
BS04 PO4 A S102 R166 D327 H331 H412 S99 R163 D324 H328 H409
BS05 PO4 A H153 R166 Y169 H150 R163 Y166
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:2anh, PDBe:2anh, PDBj:2anh
PDBsum2anh
PubMed7473737
UniProtP00634|PPB_ECOLI Alkaline phosphatase (Gene Name=phoA)

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