Structure of PDB 2zq9 Chain A

Receptor sequence
>2zq9A (length=259) Species: 562 (Escherichia coli) [Search protein sequence]
NSVQQQLEALEKSSGGRLGVALINTADNSQILYRADERFAMCSTSKVMAA
AAVLKQSESDKHLLNQRVEIKKSDLVNYNPIAEKHVNGTMTLAELGAAAL
QYSDNTAMNKLIAHLGGPDKVTAFARSLGDETFRLDRTAPTLNTAIPGDP
RDTTTPLAMAQTLKNLTLGKALAETQRAQLVTWLKGNTTGSASIRAGLPK
SWVVGDKTGSGDYGTTNDIAVIWPENHAPLVLVTYFTQPEQKAENRNDIL
AAAAKIVTH
3D structure
PDB2zq9 Structural Basis of Extend Spectrum Beta-Lactamase in Correlation of Enzymatic Kinetics and Thermal Stability of Acyl-Intermediates
ChainA
Resolution1.07 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) S70 K73 S130 A166 K234 S237
Catalytic site (residue number reindexed from 1) S43 K46 S103 A139 K207 S210
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 CEO A S70 N104 Y105 S130 P167 N170 T235 G236 S237 G238 D240 S43 N77 Y78 S103 P140 N143 T208 G209 S210 G211 D212
BS02 CLS A E273 N274 R275 D277 E244 N245 R246 D248
BS03 SPA A E96 I97 K98 N114 G115 E69 I70 K71 N87 G88
Gene Ontology
Molecular Function
GO:0008800 beta-lactamase activity
GO:0016787 hydrolase activity
Biological Process
GO:0017001 antibiotic catabolic process
GO:0030655 beta-lactam antibiotic catabolic process
GO:0046677 response to antibiotic

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Molecular Function
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Biological Process
External links
PDB RCSB:2zq9, PDBe:2zq9, PDBj:2zq9
PDBsum2zq9
PubMed
UniProtQ47066|BLT1_ECOLX Beta-lactamase Toho-1 (Gene Name=bla)

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