Structure of PDB 3sh9 Chain A

Receptor sequence
>3sh9A (length=254) Species: 1402 (Bacillus licheniformis) [Search protein sequence]
DDFAKLEEQFDAKLGIFALDTGTNRTVAYRPDERFAFASTIKALTVGVLL
QQKSIEDLNQRITYTRDDLVNYNPITEKHVDTGMTLKELADASLRYSDNA
AQNLILKQIGGPESLKKELRKIGDEVTNPERFCPNEVNPGETQDTSTARA
LVTSLRAFALEDKLPSEKRELLIDWMKRNTTGDALIRAGVPDGWEVADKT
GAASYGTRNDIAIIWPPKGDPVVLAVLSSRDKKDAKYDDKLIAEATKVVM
KALN
3D structure
PDB3sh9 Increased structural flexibility at the active site of a fluorophore-conjugated beta-lactamase distinctively impacts its binding toward diverse cephalosporin antibiotics
ChainA
Resolution1.9 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 C166 K234 A237
Catalytic site (residue number reindexed from 1) S39 K42 S97 C133 K199 A202
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 CEF A S70 S130 N132 T235 G236 A237 A238 S39 S97 N99 T200 G201 A202 A203
BS02 BB0 A V103 N104 C166 V70 N71 C133
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
Cellular Component
GO:0005886 plasma membrane

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Biological Process
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Cellular Component
External links
PDB RCSB:3sh9, PDBe:3sh9, PDBj:3sh9
PDBsum3sh9
PubMed21705325
UniProtP00808|BLAC_BACLI Beta-lactamase (Gene Name=penP)

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