Structure of PDB 1l2s Chain A

Receptor sequence
>1l2sA (length=355) Species: 562 (Escherichia coli) [Search protein sequence]
APQQINDIVHRTITPLIEQQKIPGMAVAVIYQGKPYYFTWGYADIAKKQP
VTQQTLFELGSVSKTFTGVLGGDAIARGEIKLSDPTTKYWPELTAKQWNG
ITLLHLATYTAGGLPLQVPDEVKSSSDLLRFYQNWQPAWAPGTQRLYANS
SIGLFGALAVKPSGLSFEQAMQTRVFQPLKLNHTWINVPPAEEKNYAWGY
REGKAVHVSPGALDAEAYGVKSTIEDMARWVQSNLKPLDINEKTLQQGIQ
LAQSRYWQTGDMYQGLGWEMLDWPVNPDSIINGSDNLAARPVKAITPPTP
AVRASWVHKTGATGGFGSYVAFIPEKELGIVMLANKNYPNPARVDAAWQI
LNALQ
3D structure
PDB1l2s Structure-based discovery of a novel, noncovalent inhibitor of AmpC beta-lactamase.
ChainA
Resolution1.94 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 K309 A312
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 STC A S64 N152 Y221 G317 A318 T319 G320 S61 N149 Y218 G311 A312 T313 G314 MOAD: Ki=26uM
PDBbind-CN: -logKd/Ki=4.59,Ki=26uM
BindingDB: Ki=26000nM
BS02 STC A A79 Q250 L254 S257 P306 A76 Q247 L251 S254 P300 MOAD: Ki=26uM
PDBbind-CN: -logKd/Ki=4.59,Ki=26uM
BindingDB: Ki=26000nM
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:1l2s, PDBe:1l2s, PDBj:1l2s
PDBsum1l2s
PubMed12121656
UniProtP00811|AMPC_ECOLI Beta-lactamase (Gene Name=ampC)

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