Structure of PDB 1elx Chain B

Receptor sequence
>1elxB (length=449) Species: 562 (Escherichia coli) [Search protein sequence]
TPEMPVLENRAAQGDITAPGGARRLTGDQTAALRDSLSDKPAKNIILLIG
DGMGDSEITAARNYAEGAGGFFKGIDALPLTGQYTHYALNKKTGKPDYVT
DAAASATAWSTGVKTYNGALGVDIHEKDHPTILEMAKAAGLATGNVSTAE
LQDATPAALVAHVTSRKCYGPSATSEKCPGNALEKGGKGSITEQLLNARA
DVTLGGGAKTFAETATAGEWQGKTLREQAQARGYQLVSDAASLNSVTEAN
QQKPLLGLFADGNMPVRWLGPKATYHGNIDKPAVTCTPNPQRNDSVPTLA
QMTDKAIELLSKNEKGFFLQVEGASIDKQDHAANPCGQIGETVDLDEAVQ
RALEFAKKEGNTLVIVTADHAHASQIVAPDTKAPGLTQALNTKDGAVMVM
SYGNSEEDSQEHTGSQLRIAAYGPHAANVVGLTDQTDLFYTMKAALGLK
3D structure
PDB1elx Kinetic and X-ray structural studies of three mutant E. coli alkaline phosphatases: insights into the catalytic mechanism without the nucleophile Ser102.
ChainB
Resolution2.6 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 A102 D153 T155 R166 E322 D327 K328 H331 D369 H370 H412
Catalytic site (residue number reindexed from 1) D51 A102 D153 T155 R166 E322 D327 K328 H331 D369 H370 H412
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 B D327 H331 H412 D327 H331 H412
BS02 ZN B D51 D369 H370 D51 D369 H370
BS03 MG B D51 T155 E322 D51 T155 E322
BS04 PO4 B A102 R166 D327 H412 A102 R166 D327 H412
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:1elx, PDBe:1elx, PDBj:1elx
PDBsum1elx
PubMed9533886
UniProtP00634|PPB_ECOLI Alkaline phosphatase (Gene Name=phoA)

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