Structure of PDB 1erq Chain A

Receptor sequence
>1erqA (length=263) Species: 562 (Escherichia coli) [Search protein sequence]
HPETLVKVKDAEDQLGARVGYIELDLNSGKILESFRPEERFPMMSTFKVL
LCGAVLSRVDAGQEQLGRRIHYSQNDLVEYSPVTEKHLTDGMTVRELCSA
AITMSDNTAANLLLTTIGGPKELTAFLHNMGDHVTRLDRWEPELNEAIPN
DERDTTMPAAMATTLRKLLTGELLTLASRQQLIDWMEADKVAGPLLRSAL
PAGWFIADKSGAGERGSRGIIAALGPDGKPSRIVVIYTTGSQATMDERNR
QIAEIGASLIKHW
3D structure
PDB1erq Structure-based design guides the improved efficacy of deacylation transition state analogue inhibitors of TEM-1 beta-Lactamase(,).
ChainA
Resolution1.9 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 A237
Catalytic site (residue number reindexed from 1) S45 K48 S105 E141 K209 A212
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 BJH A M69 S70 K73 Y105 S130 N132 E166 N170 S235 G236 A237 R243 M44 S45 K48 Y80 S105 N107 E141 N145 S210 G211 A212 R218 PDBbind-CN: -logKd/Ki=7.89,Ki=13nM
Gene Ontology
Molecular Function
GO:0005515 protein binding
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:1erq, PDBe:1erq, PDBj:1erq
PDBsum1erq
PubMed10820001
UniProtP62593|BLAT_ECOLX Beta-lactamase TEM (Gene Name=bla)

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