Structure of PDB 1anj Chain A

Receptor sequence
>1anjA (length=446) Species: 562 (Escherichia coli) [Search protein sequence]
MPVLENRAAQGDITAPGGARRLTGDQTAALRDSLSDKPAKNIILLIGDGM
GDSEITAARNYAEGAGGFFKGIDALPLTGQYTHYALNKKTGKPDYVTDSA
ASATAWSTGVKTYNGALGVDIHEKDHPTILEMAKAAGLATGNVSTAELQD
ATPAALVAHVTSRKCYGPSATSEKCPGNALEKGGKGSITEQLLNARADVT
LGGGAKTFAETATAGEWQGKTLREQAQARGYQLVSDAASLNSVTEANQQK
PLLGLFADGNMPVRWLGPKATYHGNIDKPAVTCTPNPQRNDSVPTLAQMT
DKAIELLSKNEKGFFLQVEGASIDHQDHAANPCGQIGETVDLDEAVQRAL
EFAKKEGNTLVIVTADHAHASQIVAPDTKAPGLTQALNTKDGAVMVMSYG
NSEEDSQEHTGSQLRIAAYGPHAANVVGLTDQTDLFYTMKAALGLK
3D structure
PDB1anj 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
Resolution2.3 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) D51 S102 D153 T155 R166 E322 D327 H328 H331 D369 H370 H412
Catalytic site (residue number reindexed from 1) D48 S99 D150 T152 R163 E319 D324 H325 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 T155 E322 D48 T152 E319
BS04 PO4 A D101 S102 R166 H331 H412 D98 S99 R163 H328 H409
BS05 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

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:1anj, PDBe:1anj, PDBj:1anj
PDBsum1anj
PubMed7473737
UniProtP00634|PPB_ECOLI Alkaline phosphatase (Gene Name=phoA)

[Back to BioLiP]