Structure of PDB 1i2w Chain B

Receptor sequence
>1i2wB (length=256) Species: 1402 (Bacillus licheniformis) [Search protein sequence]
KDDFAKLEEQFDAKLGIFALDTGTNRTVTYRPDERFAFASTIKALTVGVL
LQQKSIEDLNQRITYTRDDLVNYNPITEKHVDTGMTLKELADASLRYSDN
TAQNLILKQIGGPESLKKELRKIGDEVTNPERFEPELNEVNPGETQDTST
ARALATSLQAFALEDKLPSEKRELLIDWMKRNTTGDALIRAGVPEGWEVA
DKTGAGSYGTRNDIAIIWPPKGDPVVLAVLSSRDKKDAKYDDKLIAEATK
VVLKAL
3D structure
PDB1i2w Crystal structures of the Bacillus licheniformis BS3 class A beta-lactamase and of the acyl-enzyme adduct formed with cefoxitin
ChainB
Resolution1.7 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) S40 K43 S98 E134 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 1QL B A69 S70 K73 S130 N132 E166 P167 N170 T216 T235 G236 A237 R244 A39 S40 K43 S98 N100 E134 P135 N138 T184 T203 G204 A205 R211
Gene Ontology
Molecular Function
GO:0008800 beta-lactamase 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:1i2w, PDBe:1i2w, PDBj:1i2w
PDBsum1i2w
PubMed11827533
UniProtP00808|BLAC_BACLI Beta-lactamase (Gene Name=penP)

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