Structure of PDB 1fcn Chain A

Receptor sequence
>1fcnA (length=352) Species: 562 (Escherichia coli) [Search protein sequence]
APQQINDIVHRTITPLIEQQKIPGMAVAVIYQGKPYYFTWGYADIAKKQP
VTQQTLFELGSVSKTFTGVLGGDAIARGEIKLSDPTTKYWPELTAKQWNG
ITLLHLATYTAGGLPLLVPDEVKSSSDLLRFYQNWQPAWAPGTQRLEANS
SIGLFGALAVKPSGLSFEQAMQTRVFQPLKLNHTWINVPPAEEKNYAWGY
REGKAVHVSPGALDAEAYGVKSTIEDMARWVQSNLKPLDINEKTLQQGIQ
LAQSRYWQTGDMYQGLGWEMLDWPVNPDSIIIALAARPVKAITPPTPAVR
ASWVHKTGATGGFGSYVAFIPEKELGIVMLANKNYPNPARVDAAWQILNA
LQ
3D structure
PDB1fcn Crystal Structures of Substrate and Inhibitor Complexes with AmpC -Lactamase: Possible Implications for Substrate-Assisted Catalysis
ChainA
Resolution2.35 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) S61 K64 Y109 A111 V118 E147 A148 G153 E269 K312 A315
Catalytic site (residue number reindexed from 1) S61 K64 Y109 A111 V118 E147 A148 G153 E269 K306 A309
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 LOR A S61 L116 L117 N149 Y218 G314 A315 S61 L116 L117 N149 Y218 G308 A309
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
External links
PDB RCSB:1fcn, PDBe:1fcn, PDBj:1fcn
PDBsum1fcn
PubMed
UniProtP00811|AMPC_ECOLI Beta-lactamase (Gene Name=ampC)

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