Structure of PDB 5za2 Chain A

Receptor sequence
>5za2A (length=354) Species: 562 (Escherichia coli) [Search protein sequence]
LTATVDGIIQPMLKAYRIPGMAVAVLKDGKAHYFNYGVANRESGQRVSEQ
TLFEIGSVSKTLTATLGAYAAVKGGFELDDKVSQHAPWLKGSAFDGVTMA
ELATYSAGGLPLQFPDEVDSNDKMQTYYRSWSPVYPAGTHRQYSNPSIGL
FGHLAANSLGQPFEQLMSQTLLPKLGLHHTYIQVPESAMANYAYGYSKED
KPIRATPGVLAAEAYGIKTGSADLLKFVEANMGYQGDAALKSAIALTHTG
FHSVGEMTQGLGWESYDYPVTEQVLLAGNSPAVSFQANPVTRFAVPKAMG
EQRLYNKTGSTGGFGAYVAFVPARGIAIVMLANRNYPIEARVKAAHAILS
QLAE
3D structure
PDB5za2 Probing the Mechanism of Inactivation of the FOX-4 Cephamycinase by Avibactam
ChainA
Resolution1.503 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) S64 K67 Y150 E271 K314 S317
Catalytic site (residue number reindexed from 1) S57 K60 Y143 E264 K307 S310
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 NXL A S64 L119 Y150 T315 G316 S317 S57 L112 Y143 T308 G309 S310 MOAD: Kd=1700nM
PDBbind-CN: -logKd/Ki=5.77,Kd=1.7uM
Gene Ontology
Molecular Function
GO:0008800 beta-lactamase activity
GO:0016787 hydrolase activity
GO:0046872 metal ion binding
Biological Process
GO:0017001 antibiotic catabolic process
GO:0046677 response to antibiotic
Cellular Component
GO:0030288 outer membrane-bounded periplasmic space

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:5za2, PDBe:5za2, PDBj:5za2
PDBsum5za2
PubMed29439972
UniProtQ9L387

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