Structure of PDB 1vm1 Chain A

Receptor sequence
>1vm1A (length=265) Species: 573 (Klebsiella pneumoniae) [Search protein sequence]
SPQPLEQIKLSESQLSGRVGMIEMDLASGRTLTAWRADERFPMMSTFKVV
LCGAVLARVDAGDEQLERKIHYRQQDLVDYSPVSEKHLADGMTVGELCAA
AITMSDNSAANLLLATVGGPAGLTAFLRQIGDNVTRLDRWETELNEALPG
DARDTTTPASMAATLRKLLTSQRLSARSQRQLLQWMVDDRVAGPLIRSVL
PAGWFIADKTGAGERGARGIVALLGPNNKAERIVVIYLRDTPASMAERNQ
QIAGIGAALIEHWQR
3D structure
PDB1vm1 Inhibition of the SHV-1 beta-lactamase by sulfones: crystallographic observation of two reaction intermediates with tazobactam.
ChainA
Resolution2.02 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 MA4 A V224 P226 V261 A284 E288 V199 P201 V234 A257 E261
BS02 TBE A S70 Y105 N132 T167 N170 G236 A237 S45 Y80 N107 T142 N145 G211 A212
BS03 TAZ A Y105 E110 Y80 E85 BindingDB: Ki=2.2e+2nM,IC50=222nM
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

View graph for
Molecular Function

View graph for
Biological Process
External links
PDB RCSB:1vm1, PDBe:1vm1, PDBj:1vm1
PDBsum1vm1
PubMed11327849
UniProtP0AD64|BLA1_KLEPN Beta-lactamase SHV-1 (Gene Name=bla)

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