Structure of PDB 3b3x Chain B

Receptor sequence
>3b3xB (length=255) Species: 1402 (Bacillus licheniformis) [Search protein sequence]
DDFAKLEEQFDAKLGIFALDTGTNRTVTYRPDERFAFASTIKALTVGVLL
QQKSIEDLNQRITYTRDDLVNYNPITEKHVDTGMTLKELADASLRYSDNT
AQNLILKQIGGPESLKKELRKIGDEVTNPERFEPELNEVNPGETQDTSTA
RALATSLQAFALEDKLPSEKRELLIDWMKRNTTGDALIRAGVPEGWEVAD
KTGAGSYGTRNDIAIIWPPKGDPVVLAVLSSRDKKDAKYDDKLIAEATKV
VVKAL
3D structure
PDB3b3x 2-Aminopropane-1,2,3-tricarboxylic acid: Synthesis and co-crystallization with the class A beta-lactamase BS3 of Bacillus licheniformis
ChainB
Resolution2.5 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) S39 K42 S97 E133 K201 A204
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 A33 B S70 S130 T235 A237 R244 Y274 S39 S97 T202 A204 R210 Y239
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:3b3x, PDBe:3b3x, PDBj:3b3x
PDBsum3b3x
PubMed18515103
UniProtP00808|BLAC_BACLI Beta-lactamase (Gene Name=penP)

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