Structure of PDB 2q9n Chain A

Receptor sequence
>2q9nA (length=359) Species: 550 (Enterobacter cloacae) [Search protein sequence]
PVSEKQLAEVVANTITPLMKAQSVPGMAVAVIYQGKPHYYTFGKADIAAN
KPVTPQTLFELGSISKTFTGVLGGDAIARGEISLDDAVTRYWPQLTGKQW
QGIRMLDLATYTAGGLPLQVPDEVTDNASLLRFYQNWQPQWKPGTTRLYA
NASIGLFGALAVKPSGMPYEQAMTTRVLKPLKLDHTWINVPKAEEAHYAW
GYRDGKAVRVSPGMLDAQAYGVKTNVQDMANWVMANMAPENVADASLKQG
IALAQSRYWRIGSMYQGLGWEMLNWPVEANTVVEGSDSKVALAPLPVAEV
NPPAPPVKASWVHKTGSTGGFGSYVAFIPEKQIGIVMLANTSYPNPARVE
AAYHILEAL
3D structure
PDB2q9n 4-Substituted Trinems as Broad Spectrum beta-Lactamase Inhibitors: Structure-Based Design, Synthesis, and Biological Activity
ChainA
Resolution2.2 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 V121 Y150 G156 E272 K315 S318
Catalytic site (residue number reindexed from 1) S63 K66 Y111 V120 Y149 G155 E271 K314 S317
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 LK5 A S64 L119 Q120 Y150 N152 R204 Y221 G317 S318 T319 G320 S63 L118 Q119 Y149 N151 R203 Y220 G316 S317 T318 G319 PDBbind-CN: -logKd/Ki=6.37,IC50=430nM
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:2q9n, PDBe:2q9n, PDBj:2q9n
PDBsum2q9n
PubMed17665896
UniProtP05364|AMPC_ENTCL Beta-lactamase (Gene Name=ampC)

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