Structure of PDB 1rql Chain A

Receptor sequence
>1rqlA (length=257) Species: 1396 (Bacillus cereus) [Search protein sequence]
KIEAVIFDWAGTTVDYGCFAPLEVFMEIFHKRGVAITAEEARKPMGLLKI
DHVRALTEMPRIASEWNRVFRQLPTEADIQEMYEEFEEILFAILPRYASP
INAVKEVIASLRERGIKIGSTTGYTREMMDIVAKEAALQGYKPDFLVTPD
DVPAGRPYPWMCYKNAMELGVYPMNHMIKVGDTVSDMKEGRNAGMWTVGV
ILGSSELGLTEEEVENMDSVELREKIEVVRNRFVENGAHFTIETMQELES
VMEHIEK
3D structure
PDB1rql X-ray crystallographic and site-directed mutagenesis analysis of the mechanism of Schiff-base formation in phosphonoacetaldehyde hydrolase catalysis
ChainA
Resolution2.4 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
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 MG A D12 A14 D186 D8 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

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:1rql, PDBe:1rql, PDBj:1rql
PDBsum1rql
PubMed14670958
UniProtO31156|PHNX_BACCE Phosphonoacetaldehyde hydrolase (Gene Name=phnX)

[Back to BioLiP]