BioLiP

Structure of PDB 1c3b Chain B

Receptor sequence

>1c3bB (length=358) Species: 83333 (Escherichia coli K-12) [Search protein sequence]

APQQINDIVHRTITPLIEQQKIPGMAVAVIYQGKPYYFTWGYADIAKKQP
VTQQTLFELGSVSKTFTGVLGGDAIARGEIKLSDPTTKYWPELTAKQWNG
ITLLHLATYTAGGLPLQVPDEVKSSSDLLRFYQNWQPAWAPGTQRLYANS
SIGLFGALAVKPSGLSFEQAMQTRVFQPLKLNHTWINVPPAEEKNYAWGY
REGKAVHVSPGALDAEAYGVKSTIEDMARWVQSNLKPLDINEKTLQQGIQ
LAQSRYWQTGDMYQGLGWEMLDWPVNPDSIINGSDNKIALAARPVKAITP
PTPAVRASWVHKTGATGGFGSYVAFIPEKELGIVMLANKNYPNPARVDAA
WQILNALQ

3D structure

PDB

1c3b The complexed structure and antimicrobial activity of a non-beta-lactam inhibitor of AmpC beta-lactamase.

Chain

Resolution

2.25 Å

3D
structure

Catalytic site residues are labeled in the structure
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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	BZB	B	S64 Q120 Y150 N152 Y221 G317 A318	S61 Q117 Y147 N149 Y218 G314 A315	BindingDB: IC50=200nM,Ki=27nM

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

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Molecular Function

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Biological Process

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Cellular Component

PDB	RCSB:1c3b, PDBe:1c3b, PDBj:1c3b
PDBsum	1c3b
PubMed	10595535
UniProt	P00811\|AMPC_ECOLI Beta-lactamase (Gene Name=ampC)