Structure of PDB 5ee8 Chain A

Receptor sequence
>5ee8A (length=265) Species: 573 (Klebsiella pneumoniae) [Search protein sequence]
SPQPLEQIKLSESQLSGRVGMIEMDLASGRTLTAWRADERFPMMSTFKVV
LCGAVLARVDAGDEQLERKIHYRQQDLVDYSPVSEKHLADGMTVGELCAA
AITMSDNSAANLLLATVGGPAGLTAFLRQIGDNVTRLDRWETELNEALPG
DARDTTTPASMAATLRKLLTSQRLSARSQRQLLQWMVDDRVAGPLIRSVL
PAGWFIADKTGAGERGARGIVALLGPNNKAERIVVIYLRDTPASMAERNQ
QIAGIGAALIEHWQR
3D structure
PDB5ee8 Crystal Structures of KPC-2 and SHV-1 beta-Lactamases in Complex with the Boronic Acid Transition State Analog S02030.
ChainA
Resolution1.54 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) S70 K73 S130 E166 K234 A237
Catalytic site (residue number reindexed from 1) S45 K48 S105 E141 K209 A212
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 ZXM A M69 S70 S130 N132 E166 T167 N170 T235 A237 R243 M44 S45 S105 N107 E141 T142 N145 T210 A212 R218 PDBbind-CN: -logKd/Ki=6.89,IC50=0.13uM
BS02 MA4 A I221 V224 P226 A247 V259 A278 A282 E286 I196 V199 P201 A222 V234 A253 A257 E261
BS03 MA4 A S26 R243 Q275 A278 G279 S1 R218 Q250 A253 G254
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
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Biological Process
External links
PDB RCSB:5ee8, PDBe:5ee8, PDBj:5ee8
PDBsum5ee8
PubMed26729491
UniProtP0AD64|BLA1_KLEPN Beta-lactamase SHV-1 (Gene Name=bla)

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