Structure of PDB 1rk5 Chain A Binding Site BS02

Receptor Information

>1rk5 Chain A (length=474) Species: 511 (Alcaligenes faecalis)

PFDYILSGGTVIDGTNAPGRLADVGVRGDRIAAVGDLSASSARRRIDVAG
KVVSPGFIDSHTHDDNYLLKHRDMTPKISQGVTTVVTGNCGISLAPLAHA
NPPAPLDLLDEGGSFRFARFSDYLEALRAAPPAVNAACMVGHSTLRAAVM
PDLRREATADEIQAMQALADDALASGAIGISTGAFYPPAAHASTEEIIEV
CRPLITHGGVYATHMRDEGEHIVQALEETFRIGRELDVPVVISHHKVMGK
LNFGRSKETLALIEAAMASQDVSLDAYPYVAGSTMLKQDRVLLAGRTLIT
WCKPYPELSGRDLEEIAAERGKSKYDVVPELQPAGAIYFMMDEPDVQRIL
AFGPTMIGSAGLPHDERPHPRLWGTFPRVLGHYSRDLGLFPLETAVWKMT
GLTAAKFGLAERGQVQPGYYADLVVFDPATVADSATFEHPTERAAGIHSV
YVNGAAVWEDQSFTGQHAGRVLNR

Ligand information

• Ligand ID: CU
• InChI: InChI=1S/Cu/q+2
• InChIKey: JPVYNHNXODAKFH-UHFFFAOYSA-N
• SMILES:
  ACDLabs 10.04
  OpenEye OEToolkits 1.5.0: [Cu+2]
  CACTVS 3.341: [Cu++]
• Formula: Cu
• Name: COPPER (II) ION
• DrugBank: DB14552
• PDB chain: 1rk5 Chain A Residue 602

Receptor-Ligand Complex Structure

Structure summary

• PDB: 1rk5 The functional role of the binuclear metal center in D-aminoacylase: one-metal activation and second-metal attenuation.
• Resolution: 1.8 Å
• Binding residue (original residue number in PDB): H67 H69 C96
• Binding residue (residue number reindexed from 1): H61 H63 C90
• Annotation score: 1

Enzymatic activity

• Enzyme Commision number: 3.5.1.81: N-acyl-D-amino-acid deacylase.

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

External links

• PDB: RCSB:1rk5, PDBe:1rk5, PDBj:1rk5
• PDBsum: 1rk5
• PubMed: 14736882
• UniProt: Q9AGH8