Structure of PDB 5ew0 Chain B

Receptor sequence
>5ew0B (length=228) Species: 47917 (Serratia fonticola) [Search protein sequence]
NLTLTHFKGPLYIVEDKEYVQENSMVYIGTDGITIIGATWTPETAETLYK
EIRKVSPLPINEVINTNYHTDRAGGNAYWKTLGAKIVATQMTYDLQKSQW
GSIVNFTRQGNNKYPNLEKSLPDTVFPGDFNLQNGSIRAMYLGEAHTKDG
IFVYFPAERVLYGNCILKENLGNMSFANRTEYPKTLEKLKGLIEQGELKV
DSIIAGHDTPIHDVGLIDHYLTLLEKAP
3D structure
PDB5ew0 Cross-class metallo-beta-lactamase inhibition by bisthiazolidines reveals multiple binding modes.
ChainB
Resolution1.3 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) N107 H109 D111 H186 C205 K208 N213 H247
Catalytic site (residue number reindexed from 1) N67 H69 D71 H146 C165 K168 N173 H207
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 ZN B D111 C205 H247 D71 C165 H207
BS02 3C7 B W80 H109 D111 F146 T147 H186 C205 N213 H247 W40 H69 D71 F106 T107 H146 C165 N173 H207 MOAD: Ki=0.26uM
Gene Ontology
Molecular Function
GO:0008270 zinc ion binding
GO:0008800 beta-lactamase activity
GO:0016787 hydrolase activity
GO:0046872 metal ion binding
Biological Process
GO:0017001 antibiotic catabolic process
GO:0046677 response to antibiotic
Cellular Component
GO:0042597 periplasmic space

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Molecular Function
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Cellular Component
External links
PDB RCSB:5ew0, PDBe:5ew0, PDBj:5ew0
PDBsum5ew0
PubMed27303030
UniProtQ9RMI1

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