Structure of PDB 2aut Chain D

Receptor sequence
>2autD (length=210) [Search protein sequence]
PSTLNPGTNVAKLAEQAPVHWVSVAQIENSLTGRPPMAVGFDIDDTVLFS
SPGFWRGKKTYSPDSDDYLKNPAFWEKMNNGWDEFSIPKEAARQLIDMHV
RRGDSIYFVTGRSQTKTETVSKTLADNFHIPAANMNPVIFAGDKPEQNTN
VQWLQEKNMRIFYGDSDNDITAARDCGIRGIRILRAANSTYKPLPQAGAF
GEEVIVNSEY
3D structure
PDB2aut Structural and mutational analyses reveal the functional role of active-site Lys-154 and Asp-173 of Salmonella typhimurium AphA protein.
ChainD
Resolution2.25 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 3.1.3.2: acid 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 MG D D46 D48 D169 D42 D44 D165
BS02 PO4 D D46 I47 D48 T114 G115 D42 I43 D44 T110 G111
Gene Ontology
Molecular Function
GO:0003993 acid phosphatase activity
GO:0016787 hydrolase activity
GO:0046872 metal ion binding
Cellular Component
GO:0030288 outer membrane-bounded periplasmic space
GO:0042597 periplasmic space

View graph for
Molecular Function

View graph for
Cellular Component
External links
PDB RCSB:2aut, PDBe:2aut, PDBj:2aut
PDBsum2aut
PubMed17570338
UniProtQ540U1|APHA_SALTM Class B acid phosphatase (Gene Name=aphA)

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