Structure of PDB 1nxy Chain A

Receptor sequence
>1nxyA (length=263) Species: 562 (Escherichia coli) [Search protein sequence]
HPETLVKVKDAEDQLGARVGYIELDLNSGKILESFRPEERFPMMSTFKVL
LCGAVLSRVDAGQEQLGRRIHYSQNDLVEYSPVTEKHLTDGMTVRELCSA
AITMSDNTAANLLLTTIGGPKELTAFLHNMGDHVTRLDRWEPELNEAIPN
DERDTTTPAAMATTLRKLLTGELLTLASRQQLIDWMEADKVAGPLLRSAL
PAGWFIADKSGAGERGSRGIIAALGPDGKPSRIVVIYTTGSQATMDERNR
QIAEIGASLIKHW
3D structure
PDB1nxy Recognition and Resistance in TEM beta-lactamase
ChainA
Resolution1.6 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 SM2 A M69 S70 Y105 S130 N132 E166 N170 S235 G236 A237 G238 R244 M44 S45 Y80 S105 N107 E141 N145 S210 G211 A212 G213 R218 PDBbind-CN: -logKd/Ki=7.19,Ki=64nM
BS02 SM2 A R241 G267 S268 Q269 R215 G240 S241 Q242 PDBbind-CN: -logKd/Ki=7.19,Ki=64nM
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:1nxy, PDBe:1nxy, PDBj:1nxy
PDBsum1nxy
PubMed12859188
UniProtP62593|BLAT_ECOLX Beta-lactamase TEM (Gene Name=bla)

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