Structure of PDB 7z2y Chain A

Receptor sequence
>7z2yA (length=405) Species: 562 (Escherichia coli) [Search protein sequence]
LKLESVVIVSRHGVRAPTKATQLMQDVTPDAWPTWPVKLGWLTPRGGELI
AYLGHYQRQRLVADGLLAKKGCPQSGQVAIIADVDERTRKTGEAFAAGLA
PDCAITVHTQADTSSPDPLFNPLKTGVCQLDNANVTDAILSRAGGSIADF
TGHRQTAFRELERVLNFPQSNLCLKREKQDESCSLTQALPSELKVSADNV
SLTGAVSLASMLTEIFLLQQAQGMPEPGWGRITDSHQWNTLLSLHNAQFY
LLQRTPEVARSRATPLLDLIKTALTPHPPQKQAYGVTLPTSVLFIAGHDE
NLANLGGALELNWTLPGQPDNTPPGGELVFERWRRLSDNSQWIQVSLVFQ
TLQQMRDKTPLSLNTPPGEVKLTLAGCEERNAQGMCSLAGFTQIVNEARI
PACSL
3D structure
PDB7z2y Insights to the Structural Basis for the Stereospecificity of the Escherichia coli Phytase, AppA.
ChainA
Resolution1.86 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 R340 S342 N386 A387 Q388 R335 S337 N381 A382 Q383
BS02 IHS A R16 H17 R20 T23 K24 R92 M216 E219 F254 H303 D304 E305 R11 H12 R15 T18 K19 R87 M211 E214 F249 H298 D299 E300
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:7z2y, PDBe:7z2y, PDBj:7z2y
PDBsum7z2y
PubMed35683026
UniProtP07102|PPA_ECOLI Phytase AppA (Gene Name=appA)

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