Structure of PDB 8hpc Chain F

Receptor sequence
>8hpcF (length=299) Species: 252128 (Agrobacterium sp. KNK712) [Search protein sequence]
RQMILAVGQQGPIARAETREQVVVRLLDMLTKAASRGANFIVFPELALTT
FFPRWHFTDEAELDSFYETEMPGPVVRPLFEKAAELGIGFNLGYAELVVE
KRRFNTSILVDKSGKIVGKYRKIHLPGHKEYEAYRPFQHLEKRYFEPGDL
GFPVYDVDAAKMGMFIANDRRWPEAWRVMGLRGAEIICGGYNTPTHNPPV
PQHDHLTSFHHLLSMQAGSYQNGAWSAAAGKVGMEENCMLLGHSCIVAPT
GEIVALTTTLEDEVITAAVDLDRCRELREHIFNFKQHRQPQHYGLIAEL
3D structure
PDB8hpc Production of D-p-hydroxyphenylglycine by double-enzyme cascade
ChainF
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 F E67 K147 P151 H164 E166 A192 N193 R195 R196 N217 N222 E45 K122 P126 H139 E141 A167 N168 R170 R171 N192 N197
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

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Molecular Function
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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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