Structure of PDB 1fez Chain D

Receptor sequence
>1fezD (length=256) Species: 1396 (Bacillus cereus) [Search protein sequence]
KIEAVIFDWAGTTVDYGCFAPLEVFMEIFHKRGVAITAEEARKPMGLLKI
DHVRALTEMPRIASEWNRVFRQLPTEADIQEMYEEFEEILFAILPRYASP
INAVKEVIASLRERGIKIGSTTGYTREMMDIVAKEAALQGYKPDFLVTPD
DVPAGRPYPWMCYKNAMELGVYPMNHMIKVGDTVSDMKEGRNAGMWTVGV
ILGSSELGLTEEEVENMDSVELREKIEVVRNRFVENGAHFTIETMQELES
VMEHIE
3D structure
PDB1fez The crystal structure of bacillus cereus phosphonoacetaldehyde hydrolase: insight into catalysis of phosphorus bond cleavage and catalytic diversification within the HAD enzyme superfamily.
ChainD
Resolution3.0 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D12 A14 A45 M49 K53 H56 R160 D186
Catalytic site (residue number reindexed from 1) D8 A10 A41 M45 K49 H52 R156 D182
Enzyme Commision number 3.11.1.1: phosphonoacetaldehyde hydrolase.
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 WO4 D D12 W13 A14 T126 G127 R160 D8 W9 A10 T122 G123 R156
BS02 MG D A14 D186 A10 D182
Gene Ontology
Molecular Function
GO:0000287 magnesium ion binding
GO:0003824 catalytic activity
GO:0016787 hydrolase activity
GO:0046872 metal ion binding
GO:0050194 phosphonoacetaldehyde hydrolase activity
Biological Process
GO:0019700 organic phosphonate catabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:1fez, PDBe:1fez, PDBj:1fez
PDBsum1fez
PubMed10956028
UniProtO31156|PHNX_BACCE Phosphonoacetaldehyde hydrolase (Gene Name=phnX)

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