Structure of PDB 4yji Chain A

Receptor sequence
>4yjiA (length=490) Species: 641298 (bacterium CSBL00001) [Search protein sequence]
SPVHWKSAAEIVELVKSKQISPREVVESTIDLIEQRDPGLNAVVYKAYDE
AREKAAALERRIMQGEPVGMLAGVPTLMKDLFAAKPGWPSTLGGIRALKD
ARGAAGVWSTYPLKMSGEDSLLLGQTNSPVYGFRGTTDNTFFGPTRNPFN
LDFNAGGSSGGAAALVADGIVPVAGGTDGGGAIRIPAAWTNTYGFQPSIG
RVPFKSRPNAFHPGPYLYEGPITRTVRDAALAMNVLHGFDRRDPASLRVK
LDFTSALAQGVRGKKIGLTLNYGVFPVQQEIQDLIGKAARVFTELGAHVE
FVDLGIPYSQKQMSDAWCRMIAIPTVASMQALRKEGIDLYGEHRADIPDA
LMKWIDAVADISVQQISADQLLRTTVFDCMNGVFDRFDLLLAPTLACMPV
RNATDGCTEGPSQINGEEIDPLIGWCMTYLTNFSGHPSASVPAGLIDGLP
AGMLIIGDRQADLDVIAASAAFERASPWSQYYDIPAGRPL
3D structure
PDB4yji Crystal structure analysis of a bacterial aryl acylamidase belonging to the amidase signature enzyme family
ChainA
Resolution1.73 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) K84 S163 S164 G184 G185 G186 A187
Catalytic site (residue number reindexed from 1) K79 S158 S159 G179 G180 G181 A182
Enzyme Commision number 3.5.1.13: aryl-acylamidase.
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 TYL A L86 G137 S163 G184 G185 A187 L81 G132 S158 G179 G180 A182
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0016787 hydrolase activity
GO:0047680 aryl-acylamidase activity

View graph for
Molecular Function
External links
PDB RCSB:4yji, PDBe:4yji, PDBj:4yji
PDBsum4yji
PubMed26454172
UniProtC3UWD1

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