Structure of PDB 8hpc Chain D

Receptor sequence
>8hpcD (length=303) Species: 252128 (Agrobacterium sp. KNK712) [Search protein sequence]
TRQMILAVGQQGPIARAETREQVVVRLLDMLTKAASRGANFIVFPELALT
TFFPRWHFTDEAELDSFYETEMPGPVVRPLFEKAAELGIGFNLGYAELVV
EGGVKRRFNTSILVDKSGKIVGKYRKIHLPGHKEYEAYRPFQHLEKRYFE
PGDLGFPVYDVDAAKMGMFIANDRRWPEAWRVMGLRGAEIICGGYNTPTH
NPPVPQHDHLTSFHHLLSMQAGSYQNGAWSAAAGKVGMEENCMLLGHSCI
VAPTGEIVALTTTLEDEVITAAVDLDRCRELREHIFNFKQHRQPQHYGLI
AEL
3D structure
PDB8hpc Production of D-p-hydroxyphenylglycine by double-enzyme cascade
ChainD
Resolution2.52 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 3.5.1.77: N-carbamoyl-D-amino-acid 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 M9L D E67 K147 P151 H164 E166 A192 N193 R196 N217 N222 E46 K126 P130 H143 E145 A171 N172 R175 N196 N201
Gene Ontology
Molecular Function
GO:0003837 beta-ureidopropionase activity
GO:0016787 hydrolase activity
GO:0047417 N-carbamoyl-D-amino acid hydrolase activity
Biological Process
GO:0033396 beta-alanine biosynthetic process via 3-ureidopropionate

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:8hpc, PDBe:8hpc, PDBj:8hpc
PDBsum8hpc
PubMed
UniProtP60327|DCAS_AGRSK N-carbamoyl-D-amino acid hydrolase

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