Structure of PDB 1anj Chain A Binding Site BS02

Receptor Information
>1anj Chain A (length=446) Species: 562 (Escherichia coli) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
MPVLENRAAQGDITAPGGARRLTGDQTAALRDSLSDKPAKNIILLIGDGM
GDSEITAARNYAEGAGGFFKGIDALPLTGQYTHYALNKKTGKPDYVTDSA
ASATAWSTGVKTYNGALGVDIHEKDHPTILEMAKAAGLATGNVSTAELQD
ATPAALVAHVTSRKCYGPSATSEKCPGNALEKGGKGSITEQLLNARADVT
LGGGAKTFAETATAGEWQGKTLREQAQARGYQLVSDAASLNSVTEANQQK
PLLGLFADGNMPVRWLGPKATYHGNIDKPAVTCTPNPQRNDSVPTLAQMT
DKAIELLSKNEKGFFLQVEGASIDHQDHAANPCGQIGETVDLDEAVQRAL
EFAKKEGNTLVIVTADHAHASQIVAPDTKAPGLTQALNTKDGAVMVMSYG
NSEEDSQEHTGSQLRIAAYGPHAANVVGLTDQTDLFYTMKAALGLK
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 chain1anj Chain A Residue 451 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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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.
Resolution2.3 Å
Binding residue
(original residue number in PDB)		D51 S102 D369 H370
Binding residue
(residue number reindexed from 1)		D48 S99 D366 H367
Annotation score1
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.
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:1anj, PDBe:1anj, PDBj:1anj
PDBsum1anj
PubMed7473737
UniProtP00634|PPB_ECOLI Alkaline phosphatase (Gene Name=phoA)

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