Structure of PDB 1iys Chain A

Receptor sequence
>1iysA (length=261) Species: 562 (Escherichia coli) [Search protein sequence]
NSVQQQLEALEKSSGGRLGVALINTADNSQILYRADERFAMCSTSKVMAA
AAVLKQSESDKHLLNQRVEIKKSDLVNYNPIAEKHVNGTMTLAELGAAAL
QYSDNTAMNKLIAHLGGPDKVTAFARSLGDETFRLDRTEPTLNTAIPGDP
RDTTTPLAMAQTLKNLTLGKALAETQRAQLVTWLKGNTTGSASIRAGLPK
SWVVGDKTGSGDYGTTNDIAVIWPENHAPLVLVTYFTQPEQKAERRRDIL
AAAAKIVTHGF
3D structure
PDB1iys Crystal Structure of Extended-Spectrum beta-Lactamase Toho-1: Insights into the Molecular Mechanism for Catalytic Reaction and Substrate Specificity Expansion
ChainA
Resolution1.65 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 E166 K234 S237
Catalytic site (residue number reindexed from 1) S43 K46 S103 E139 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 SO4 A S70 S130 T235 G236 S237 S43 S103 T208 G209 S210
BS02 SO4 A E273 R274 R276 E244 R245 R247
BS03 SO4 A W229 E254 N255 H256 F290 W202 E225 N226 H227 F261
BS04 SO4 A H89 N92 H62 N65
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:1iys, PDBe:1iys, PDBj:1iys
PDBsum1iys
PubMed12962487
UniProtQ47066|BLT1_ECOLX Beta-lactamase Toho-1 (Gene Name=bla)

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