Structure of PDB 1pzo Chain A

Receptor sequence
>1pzoA (length=263) Species: 562 (Escherichia coli) [Search protein sequence]
HPETLVKVKDAEDQLGARVGYIELDLNSGKILESFRPEERFPMMSTFKVL
LCGAVLSRVDAGQEQLGRRIHYSQNDLVEYSPVTEKHLTDGMTVRELCSA
AITMSDNTAANLLLTTIGGPKELTAFLHNMGDHVTRLDRWEPELNEAIPN
DERDTTTPAAMATTLRKLLTGELLTLASRQQLIDWMEADKVAGPLLRSAL
PAGWFIADKSGAGERGSRGIIAALGPDGKPSRIVVIYTTGSQATMDERNR
QIAEIGASLIKHW
3D structure
PDB1pzo Allosteric inhibition through core disruption.
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 CBT A L220 S235 G236 R244 G245 I246 N276 I279 L195 S210 G211 R218 G219 I220 N249 I252 MOAD: Ki=460uM
PDBbind-CN: -logKd/Ki=3.32,Ki=480uM
BS02 CBT A L220 L221 A224 N276 I279 A280 G283 L195 L196 A199 N249 I252 A253 G256 MOAD: Ki=460uM
PDBbind-CN: -logKd/Ki=3.32,Ki=480uM
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:1pzo, PDBe:1pzo, PDBj:1pzo
PDBsum1pzo
PubMed15037085
UniProtP62593|BLAT_ECOLX Beta-lactamase TEM (Gene Name=bla)

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