Structure of PDB 1pi5 Chain B

Receptor sequence

>1pi5B (length=358) Species: 562 (Escherichia coli)

APQQINDIVHRTITPLIEQQKIPGMAVAVIYQGKPYYFTWGYADIAKKQP
VTQQTLFELGSVSKTFTGVLGGDAIARGEIKLSDPTTKYWPELTAKQWNG
ITLLHLATYTAGGLPLQVPDEVKSSSDLLRFYQNWQPAWAPGTQRLYANS
SIGLFGALAVKPSGLSFEQAMQTRVFQPLKLNHTWINVPPAEEKNYAWGY
REGKAVHVSPGALDAEAYGVKSTIEDMARWVQSNLKPLDINEKTLQQGIQ
LAQSRYWQTGDMYQGLGWEMLDWPVNPDSIINGSDAKIALAARPVKAITP
PTPAVRASWVHKTGATGGFGSYVAFIPEKELGIVMLANKNYPNPARVDAA
WQILNALQ

3D structure

• PDB: 1pi5 Thermodynamic cycle analysis and inhibitor design against beta-lactamase.
• Chain: B
• Resolution: 1.49 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	SM2	B	D281 S282 N285 G286 I291 R296	D278 S279 N282 G283 I288 R293	MOAD: Ki=17nM
BS02	SM2	B	S64 L119 Q120 Y150 Y221 G317 A318 T319 G320	S61 L116 Q117 Y147 Y218 G314 A315 T316 G317	MOAD: Ki=17nM

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:1pi5, PDBe:1pi5, PDBj:1pi5
• PDBsum: 1pi5
• PubMed: 14661960
• UniProt: P00811|AMPC_ECOLI Beta-lactamase (Gene Name=ampC)