Structure of PDB 8apz Chain B

Receptor sequence
>8apzB (length=410) Species: 382 (Sinorhizobium meliloti) [Search protein sequence]
NRRVNADRLWDSLMEMAKIGPGVAGGNNRQTLTDADGEGRRLFQSWCEEA
GLSMGVDKMGTMFLTRPGTDPDALPVHIGSHLDTQPTGGKFDGVLGVLSG
LEAVRTMNDLGIKTKHPIVVTNWTNEEGARFAPAMLASGVFAGVHTLEYA
YARKDPEGKSFGDELKRIGWLGDEEVGARKMHAYFEYHIEQGPILEAENK
QIGVVTHCQGLWWLEFTLTGREAHTGSTPMDMRVNAGLAMARILEMVQTV
AMENQPGAVGGVGQMFFSPNSRNVLPGKVVFTVDIRSPDQAKLDGMRARI
EAEAPKICERLGVGCSIEAVGHFDPVTFDPKLVETVRGAAEKLGYSHMNL
VSGAGHDACWAAKVAPTTMIMCPCVGGLSHNEAEDISREWAAAGADVLFH
AVLETAEIVE
3D structure
PDB8apz Selecting Better Biocatalysts by Complementing Recoded Bacteria.
ChainB
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 ORD B H230 N279 H224 N273
BS02 ZN B H87 D98 H194 H81 D92 H188
BS03 FE B H87 D98 G99 E132 H194 H81 D92 G93 E126 H188
BS04 ZN B D98 E133 H386 D92 E127 H380
BS05 FE B D98 E133 H386 D92 E127 H380
BS06 ORD B D98 E132 E133 H194 Q197 R292 A360 G361 D92 E126 E127 H188 Q191 R286 A354 G355
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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