Structure of PDB 4izs Chain A

Receptor sequence
>4izsA (length=261) Species: 501897 (Nesterenkonia sp. 10004) [Search protein sequence]
GLVPRGSHMRIALMQHTARPLDPQHNLDLIDDAAARASEQGAQLLLTPEL
FGFGYVPSQICAQVSAEQVDAARSRLRGIARDRGIALVWSLPGPEGPEQR
GITAELADEHGEVLASYQKVQLYGPEEKAAFVPGEQPPPVLSWGGRQLSL
LVAYDVEFPEMVRAAAARGAQLVLVPTALAGDETSVPGILLPARAVENGI
TLAYANHCGPEGGLVFDGGSVVVGPAGQPLGELGVEPGLLVVDLPADYLQ
DRRAELHRNWL
3D structure
PDB4izs 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
Resolution1.44 Å
3D
structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
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 BMD A E41 K111 Y115 E119 A145 Y146 E149 A170 E49 K119 Y123 E127 A153 Y154 E157 A178
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

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:4izs, PDBe:4izs, PDBj:4izs
PDBsum4izs
PubMed
UniProtD0VWZ1

[Back to BioLiP]