Structure of PDB 4tsr Chain A

Receptor sequence
>4tsrA (length=399) Species: 562 (Escherichia coli) [Search protein sequence]
LKLESVVIVSRHGVRAPTKATQLMQDVTPDAWPTWPVKLGWLTPRGGELI
AYLGHYQRQRLVADGLLAKKGCPQSGQVAIIADTDERTRKTGEAFAAGLA
PDCAITVHTQVDTSSPDPLFNPLKTGVCQLDNANVTDAILSRAGGSIADF
TGHRQTAFRELERVLNFPQSNLCLKRCSLTQALPSELKVSADNVALTGAV
SLASMLTEIFLLQQAQGMPEPGWGRITDSHQWNTLLSLHNAQFYLLQRTP
EVARSRATPLLDLIKTALTPHPPQKQAYGVTLPTSVLFIAGHDTNLANLG
GALELNWTLPGQPDNTPPGGELVFERWRRLSDNSQWIQVSLVFQTLQQMR
DKTPLSLNTPPGEVKLTLAGCEERNAQGMCSLAGFTQIVNEARIPACSL
3D structure
PDB4tsr The Complex Structure of mutant Phytase with IHS
ChainA
Resolution2.07 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 3.1.3.-
3.6.1.-
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 IHS A R16 H17 R20 T23 K24 R92 M216 F254 H303 D304 R11 H12 R15 T18 K19 R87 M205 F243 H292 D293
Gene Ontology
Molecular Function
GO:0003924 GTPase activity
GO:0003993 acid phosphatase activity
GO:0008252 nucleotidase activity
GO:0008707 4-phytase activity
GO:0016787 hydrolase activity
GO:0050308 sugar-phosphatase activity
GO:0052745 inositol phosphate phosphatase activity
Biological Process
GO:0016036 cellular response to phosphate starvation
GO:0071454 cellular response to anoxia
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:4tsr, PDBe:4tsr, PDBj:4tsr
PDBsum4tsr
PubMed
UniProtP07102|PPA_ECOLI Phytase AppA (Gene Name=appA)

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