Structure of PDB 5gwa Chain A

Receptor sequence
>5gwaA (length=275) Species: 615 (Serratia marcescens) [Search protein sequence]
GTDSLKNSIEKYLKDKKAKVGVAVLGIEDNFKLNVNEKHHYPMQSTYKFH
LALAVLDKLDKENISVDKKLFVKKSDLQPNTWSPLKDKYPNGNLELSFSE
IIKSTVSHSDNNGCDILFRFVGGTNKVHNFISKLGVKNISIKATEEEMHK
AWNVQYTNWTTPDATVQLLKKFYKNEILSKNSYDFLLNTMIETTTGPKRL
KGLLPDGTVVAHKTGSSDTNNKGITAATNDIGIITLPNGKHFAIAVYVSD
SSEKSDVNEKIIAEICKSVWDYLVK
3D structure
PDB5gwa Structural Insights into the TLA-3 Extended-Spectrum beta-Lactamase and Its Inhibition by Avibactam and OP0595.
ChainA
Resolution1.59 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) S56 K59 S120 E156 K224 S227
Catalytic site (residue number reindexed from 1) S45 K48 S109 E145 K213 S216
Enzyme Commision number 3.5.2.6: beta-lactamase.
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 NXL A S56 W93 S120 N122 T225 G226 S227 S45 W82 S109 N111 T214 G215 S216 PDBbind-CN: -logKd/Ki=5.77,Ki=1.71uM
BS02 SO4 A T246 H252 T235 H241
BS03 SO4 A G207 R210 E270 G196 R199 E259
Gene Ontology
Molecular Function
GO:0008800 beta-lactamase activity
GO:0016787 hydrolase activity
Biological Process
GO:0017001 antibiotic catabolic process
GO:0030655 beta-lactam antibiotic catabolic process
GO:0046677 response to antibiotic

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Molecular Function
View graph for
Biological Process
External links
PDB RCSB:5gwa, PDBe:5gwa, PDBj:5gwa
PDBsum5gwa
PubMed28739781
UniProtA0A0B6VPP7

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