Structure of PDB 4izw Chain A

Receptor sequence
>4izwA (length=262) Species: 501897 (Nesterenkonia sp. 10004) [Search protein sequence]
GLVPRGSHMRIALMQHTARPLDPQHNLDLIDDAAARASEQGAQLLLTPLL
FGFGYVPSQICAQVSAEQVDAARSRLRGIARDRGIALVWSLPGPEGPEQR
GITAELADEHGEVLASYQKVQLYGPEEKAAFVPGEQPPPVLSWGGRQLSL
LVCYDVEFPEMVRAAAARGAQLVLVPTALAGDETSVPGILLPARAVENGI
TLAYANHCGPEGGLVFDGGSVVVGPAGQPLGELGVEPGLLVVDLPDADYL
QDRRAELHRNWL
3D structure
PDB4izw 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
Resolution1.6 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 FTM A Y115 E149 Y123 E157
BS02 FTM A Y47 A170 Y55 A178
BS03 FTM A V112 Q113 L114 V120 Q121 L122
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:4izw, PDBe:4izw, PDBj:4izw
PDBsum4izw
PubMed
UniProtD0VWZ1

[Back to BioLiP]