Structure of PDB 3ly4 Chain A

Receptor sequence
>3ly4A (length=257) Species: 1402 (Bacillus licheniformis) [Search protein sequence]
KDDFAKLEEQFDAKLGIFALDTGTNRTVAYRPDERFAFASTIKALTVGVL
LQQKSIEDLNQRITYTRDDLVNYNPITEKHVDTGMTLKELADASLRYSDN
AAQNLILKQIGGPESLKKELRKIGDEVTNPERFCPELNEVNPGETQDTST
ARALVTSLRAFALEDKLPSEKRELLIDWMKRNTTGDALIRAGVPDGWEVA
DKTGAASYGTRNDIAIIWPPKGDPVVLAVLSSRDKKDAKYDDKLIAEATK
VVMKALN
3D structure
PDB3ly4 Crystal Structure of fluorophore-labeled Class A -lactamase PenP-E166Cb in complex with penicillin G
ChainA
Resolution1.8 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) S40 K43 S98 C134 K202 A205
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 PNM A S70 S130 N132 T235 G236 A237 A238 S40 S98 N100 T203 G204 A205 A206
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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Cellular Component
External links
PDB RCSB:3ly4, PDBe:3ly4, PDBj:3ly4
PDBsum3ly4
PubMed
UniProtP00808|BLAC_BACLI Beta-lactamase (Gene Name=penP)

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