Structure of PDB 4mbf Chain A

Receptor sequence
>4mbfA (length=265) Species: 573 (Klebsiella pneumoniae) [Search protein sequence]
SPQPLEQIKLSESQLSGRVGMIEMDLASGRTLTAWRADERFPMMSTFKVV
LCGAVLARVDAGDEQLERKIHYRQQDLVDYSPVSEKHLADGMTVGELCAA
AITMSDNSAANLLLATVGGPAGLTAFLRQIGDNVTRLDRWETELNEALPG
DARDTTTPASMAATLRKLLTSQRLSARSQRQLLQWMVDDRVAGPLIRSVL
PAGWFIADKTGAGERGARGIVALLGPNNKAERIVVIYLRDTPASMAERNQ
QIAGIGAALIEHWQR
3D structure
PDB4mbf Penam sulfones and beta-lactamase inhibition: SA2-13 and the importance of the C2 side chain length and composition.
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 MA4 A V224 P226 A248 V261 A280 A284 E288 V199 P201 A222 V234 A253 A257 E261
BS02 MA4 A R244 I279 R218 I252
BS03 2AW A S70 Y105 N132 N170 T235 G236 A237 R244 S45 Y80 N107 N145 T210 G211 A212 R218 PDBbind-CN: -logKd/Ki=5.77,Ki=1.7uM
BS04 2AW A V224 P226 A227 V199 P201 A202 PDBbind-CN: -logKd/Ki=5.77,Ki=1.7uM
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:4mbf, PDBe:4mbf, PDBj:4mbf
PDBsum4mbf
PubMed24454944
UniProtP0AD64|BLA1_KLEPN Beta-lactamase SHV-1 (Gene Name=bla)

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