Structure of PDB 1rjq Chain A

Receptor sequence
>1rjqA (length=474) Species: 511 (Alcaligenes faecalis) [Search protein sequence]
PFDYILSGGTVIDGTNAPGRLADVGVRGDRIAAVGDLSASSARRRIDVAG
KVVSPGFIDSHTHDDNYLLKHRDMTPKISQGVTTVVTGNCGISLAPLAHA
NPPAPLDLLDEGGSFRFARFSDYLEALRAAPPAVNAACMVGHSTLRAAVM
PDLRREATADEIQAMQALADDALASGAIGISTGAFYPPAAHASTEEIIEV
CRPLITHGGVYATHMRDEGEHIVQALEETFRIGRELDVPVVISHHKVMGK
LNFGRSKETLALIEAAMASQDVSLDAYPYVAGSTMLKQDRVLLAGRTLIT
WCKPYPELSGRDLEEIAAERGKSKYDVVPELQPAGAIYFMMDEPDVQRIL
AFGPTMIGSAGLPHDERPHPRLWGTFPRVLGHYSRDLGLFPLETAVWKMT
GLTAAKFGLAERGQVQPGYYADLVVFDPATVADSATFEHPTERAAGIHSV
YVNGAAVWEDQSFTGQHAGRVLNR
3D structure
PDB1rjq The functional role of the binuclear metal center in D-aminoacylase: one-metal activation and second-metal attenuation.
ChainA
Resolution1.8 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 3.5.1.81: N-acyl-D-amino-acid deacylase.
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 ZN A C96 H220 H250 C90 H214 H244
Gene Ontology
Molecular Function
GO:0016787 hydrolase activity
GO:0016810 hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
GO:0016811 hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides
GO:0046872 metal ion binding
GO:0047420 N-acyl-D-amino-acid deacylase activity

View graph for
Molecular Function
External links
PDB RCSB:1rjq, PDBe:1rjq, PDBj:1rjq
PDBsum1rjq
PubMed14736882
UniProtQ9AGH8

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