Structure of PDB 8aq0 Chain B

Receptor sequence
>8aq0B (length=410) Species: 382 (Sinorhizobium meliloti) [Search protein sequence]
ENRRVNADRLWDSLMEMAKIGPGVAGGNNRQTLTDADGEGRRLFQSWCEE
AGLSMGVDKMGTMFLTRPGTDPDALPVHIGSHLDTQPTGGKFDGVLGVLS
GLEAVRTMNDLGIKTKHPIVVTNWTNEEGARFAPAMLASGVFAGVHTLEY
AYARKDPEGKSFGDELKRIGWLGDEEVGARKMHAYFEYHIEQGPILEAEN
KQIGVVTHCQGGWWLEFTLTGREAHTGSTPMDMRVNAGLAMARILEMVQT
VAMENQPGAVGGVGQMFFSPNSRNVLPGKVVFTVDIRSPDQAKLDGMRAR
IEAEAPKICERLGVGCSIEAVGHCDPVTFDPKLVETVRGAAEKLGYSHMN
LVSGAGHDACWAAKVAPTTMIMCPCVGGLSHNEAEDISREWAAAGADVLF
HAVLETAEIV
3D structure
PDB8aq0 Selecting Better Biocatalysts by Complementing Recoded Bacteria.
ChainB
Resolution2.3 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 NV6 B H230 N279 H225 N274
BS02 ZN B H87 D98 H194 H82 D93 H189
BS03 FE B H87 D98 E132 H194 H82 D93 E127 H189
BS04 ZN B D98 E133 H386 D93 E128 H381
BS05 FE B D98 E133 H386 D93 E128 H381
BS06 NV6 B D98 E132 E133 A140 M141 W219 R292 A360 G361 H386 D93 E127 E128 A135 M136 W214 R287 A355 G356 H381
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:8aq0, PDBe:8aq0, PDBj:8aq0
PDBsum8aq0
PubMed36342942
UniProtQ6DTN4|HYUC_RHIML N-carbamoyl-L-amino-acid hydrolase (Gene Name=hyuC)

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