Structure of PDB 4izu Chain A

Receptor sequence
>4izuA (length=254) Species: 501897 (Nesterenkonia sp. 10004) [Search protein sequence]
HMRIALMQHTARPLDPQHNLDLIDDAAARASEQGAQLLLTPQLFGFGYVP
SQICAQVSAEQVDAARSRLRGIARDRGIALVWSLPGPEGPEQRGITAELA
DEHGEVLASYQKVQLYGPEEKAAFVPGEQPPPVLSWGGRQLSLLVCYDVE
FPEMVRAAAARGAQLVLVPTALAGDETSVPGILLPARAVENGITLAYANH
CGPEGGLVFDGGSVVVGPAGQPLGELGVEPGLLVVDLPADYLQDRRAELH
RNWL
3D structure
PDB4izu Covalent modifications of the active site cysteine occur as a result of mutating the glutamate of the catalytic triad in the amidase from Nesterenkonia sp.
ChainA
Resolution1.4 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 3.5.1.4: amidase.
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 ROP A C53 P89 E90 C54 P90 E91
BS02 ROP A Q41 Y47 K111 Y115 C145 Y146 Q42 Y48 K112 Y116 C146 Y147
BS03 1HC A Q16 A64 R67 Q17 A65 R68
Gene Ontology
Molecular Function
GO:0004040 amidase activity
GO:0016787 hydrolase activity
GO:0043864 indoleacetamide hydrolase activity
GO:0050126 N-carbamoylputrescine amidase activity
Biological Process
GO:0033388 putrescine biosynthetic process from arginine

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Molecular Function
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Biological Process
External links
PDB RCSB:4izu, PDBe:4izu, PDBj:4izu
PDBsum4izu
PubMed
UniProtD0VWZ1

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