Structure of PDB 1y6v Chain B Binding Site BS03

Receptor Information
>1y6v Chain B (length=449) Species: 562 (Escherichia coli) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
TPEMPVLENRAAQGDITAPGGARRLTGDQTAALRDSLSDKPAKNIILLIG
DGMGDSEITAARNYAEGAGGFFKGIDALPLTGQYTHYALNKKTGKPDYVT
DSAASATAWSTGVKTYNGALGVDIHEKDHPTILEMAKAAGLATGNVSTAE
LQDATPAALVAHVTSRKCYGPSATSEKCPGNALEKGGKGSITEQLLNARA
DVTLGGGAKTFAETATAGEWQGKTLREQAQARGYQLVSDAASLNSVTEAN
QQKPLLGLFADGNMPVRWLGPKATYHGNIDKPAVTCTPNPQRNDSVPTLA
QMTDKAIELLSKNEKGFFLQVEGASIDKQDHAANPCGQIGETVDLDEAVQ
RALEFAKKEGNTLVIVTADHAHASQIVAPDTKAPGLTQALNTKDGAVMVM
SYGNSEEDSQEHTGSQLRIAAYGPHAANVVGLTDQTDLFYTMKAALGLK
Ligand information
Ligand IDCO
InChIInChI=1S/Co/q+2
InChIKeyXLJKHNWPARRRJB-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0		[Co+2]
CACTVS 3.341[Co++]
FormulaCo
NameCOBALT (II) ION
ChEMBL
DrugBankDB14205
ZINC
PDB chain1y6v Chain B Residue 952 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB1y6v Metal Specificity Is Correlated with Two Crucial Active Site Residues in Escherichia coli Alkaline Phosphatase(,).
Resolution1.6 Å
Binding residue
(original residue number in PDB)		D51 T155 E322
Binding residue
(residue number reindexed from 1)		D51 T155 E322
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) D51 S102 D153 T155 R166 E322 D327 K328 H331 D369 H370 H412
Catalytic site (residue number reindexed from 1) D51 S102 D153 T155 R166 E322 D327 K328 H331 D369 H370 H412
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:1y6v, PDBe:1y6v, PDBj:1y6v
PDBsum1y6v
PubMed15938627
UniProtP00634|PPB_ECOLI Alkaline phosphatase (Gene Name=phoA)

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