Structure of PDB 3bls Chain B

Receptor sequence

>3blsB (length=357) Species: 83333 (Escherichia coli K-12)

APQQINDIVHRTITPLIEQQKIPGMAVAVIYQGKPYYFTWGYADIAKKQP
VTQQTLFELGSVSKTFTGVLGGDAIARGEIKLSDPTTKYWPELTAKQWNG
ITLLHLATYTAGGLPLQVPDEVKSSSDLLRFYQNWQPAWAPGTQRLYANS
SIGLFGALAVKPSGLSFEQAMQTRVFQPLKLNHTWINVPPAEEKNYAWGY
REGKAVHVSPGALDAEAYGVKSTIEDMARWVQSNLKPLDINEKTLQQGIQ
LAQSRYWQTGDMYQGLGWEMLDWPVNPDSIINGSDNKIALAARPVKAITP
PTPAVRASWVHKTGATGGFGSYVAFIPEKELGIVMLANKNYPNPARVDAA
WQILNAL

3D structure

• PDB: 3bls Three-dimensional structure of AmpC beta-lactamase from Escherichia coli bound to a transition-state analogue: possible implications for the oxyanion hypothesis and for inhibitor design.
• Chain: B
• Resolution: 2.3 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): S64 K67 Y112 A114 V121 Y150 G156 E272 K315 A318
• Catalytic site (residue number reindexed from 1): S61 K64 Y109 A111 V118 Y147 G153 E269 K312 A315
• 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	APB	B	S64 Y150 T316 G317 A318 N346	S61 Y147 T313 G314 A315 N343	BindingDB: Ki=7300nM

Gene Ontology

Molecular Function

• GO:0008800 beta-lactamase activity
• GO:0016787 hydrolase activity

Biological Process

• GO:0017001 antibiotic catabolic process
• GO:0046677 response to antibiotic

Cellular Component

• GO:0030288 outer membrane-bounded periplasmic space
• GO:0042597 periplasmic space

External links

• PDB: RCSB:3bls, PDBe:3bls, PDBj:3bls
• PDBsum: 3bls
• PubMed: 9819201
• UniProt: P00811|AMPC_ECOLI Beta-lactamase (Gene Name=ampC)