Structure of PDB 8apz Chain A

Receptor sequence
>8apzA (length=412) Species: 382 (Sinorhizobium meliloti) [Search protein sequence]
GENRRVNADRLWDSLMEMAKIGPGVAGGNNRQTLTDADGEGRRLFQSWCE
EAGLSMGVDKMGTMFLTRPGTDPDALPVHIGSHLDTQPTGGKFDGVLGVL
SGLEAVRTMNDLGIKTKHPIVVTNWTNEEGARFAPAMLASGVFAGVHTLE
YAYARKDPEGKSFGDELKRIGWLGDEEVGARKMHAYFEYHIEQGPILEAE
NKQIGVVTHCQGLWWLEFTLTGREAHTGSTPMDMRVNAGLAMARILEMVQ
TVAMENQPGAVGGVGQMFFSPNSRNVLPGKVVFTVDIRSPDQAKLDGMRA
RIEAEAPKICERLGVGCSIEAVGHFDPVTFDPKLVETVRGAAEKLGYSHM
NLVSGAGHDACWAAKVAPTTMIMCPCVGGLSHNEAEDISREWAAAGADVL
FHAVLETAEIVE
3D structure
PDB8apz Selecting Better Biocatalysts by Complementing Recoded Bacteria.
ChainA
Resolution1.75 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 3.5.1.87: N-carbamoyl-L-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 ZN A H87 D98 H194 H83 D94 H190
BS02 FE A H87 D98 G99 E132 H194 H83 D94 G95 E128 H190
BS03 ZN A D98 E133 H386 D94 E129 H382
BS04 FE A D98 E133 H386 D94 E129 H382
BS05 ORD A H87 D98 E132 E133 H194 Q197 R292 A360 G361 H83 D94 E128 E129 H190 Q193 R288 A356 G357
BS06 ORD A H230 N279 H226 N275
Gene Ontology
Molecular Function
GO:0016787 hydrolase activity
GO:0016813 hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines
GO:0046872 metal ion binding
GO:0050538 N-carbamoyl-L-amino-acid hydrolase activity
Biological Process
GO:0008652 amino acid biosynthetic process

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Molecular Function
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Biological Process
External links
PDB RCSB:8apz, PDBe:8apz, PDBj:8apz
PDBsum8apz
PubMed36342942
UniProtQ6DTN4|HYUC_RHIML N-carbamoyl-L-amino-acid hydrolase (Gene Name=hyuC)

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