Structure of PDB 1kh5 Chain A

Receptor sequence

>1kh5A (length=444) Species: 562 (Escherichia coli)

VLENRAAQGNITAPGGARRLTGDQTAALRNSLSDKPAKNIILLIGDGMGD
SEITAARNYAEGAGGFFKGIDALPLTGQYTHYALNKKTGKPDYVTDSAAS
ATAWSTGVKTYNGALGVDIHEKDHPTILEMAKAAGLATGNVSTAELQDAT
PAALVAHVTSRKCYGPSATSQKCPGNALEKGGKGSITEQLLNARADVTLG
GGAKTFAETATAGEWQGKTLREEAEARGYQLVSDAASLNSVTEANQQKPL
LGLFADGNMPVRWLGPKATYHGNIDKPAVTCTPNPQRNDSVPTLAQMTDK
AIELLSKNEKGFFLQVEGASIDKQNHAANPCGQIGETVDLDEAVQRALEF
AKKEGNTLVIVTADHAHASQIVAPDTKAPGLTQALNTKDGAVMVMSYGNS
EEDSQEHTGSQLRIAAYGPHAANVVGLTDQTDLFYTMKAALGLK

3D structure

• PDB: 1kh5 Artificial evolution of an enzyme active site: structural studies of three highly active mutants of Escherichia coli alkaline phosphatase.
• Chain: A
• Resolution: 2.0 Å

Enzymatic activity

• 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	D322 H326 H407
BS02	ZN	A	D51 S102 D369 H370	D46 S97 D364 H365
BS03	MG	A	D51 T155 E322	D46 T150 E317
BS04	AF3	A	S102 R166 D327 H412	S97 R161 D322 H407

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

External links

• PDB: RCSB:1kh5, PDBe:1kh5, PDBj:1kh5
• PDBsum: 1kh5
• PubMed: 11884134
• UniProt: P00634|PPB_ECOLI Alkaline phosphatase (Gene Name=phoA)