Structure of PDB 5chm Chain A

Receptor sequence
>5chmA (length=355) Species: 562 (Escherichia coli) [Search protein sequence]
PLTATVDGIIQPMLKAYRIPGMAVAVLKDGKAHYFNYGVANRESGQRVSE
QTLFEIGSVSKTLTATLGAYAAVKGGFELDDKVSQHAPWLKGSAFDGVTM
AELATYSAGGLPLQFPDEVDSNDKMQTYYRSWSPVYPAGTHRQYSNPSIG
LFGHLAANSLGQPFEQLMSQTLLPKLGLHHTYIQVPESAMANYAYGYSKE
DKPIRATPGVLAAEAYGIKTGSADLLKFVEANMGYQGDAALKSAIALTHT
GFHSVGEMTQGLGWESYDYPVTEQVLLAGNSPAVSFQANPVTRFAVPKAM
GEQRLYNKTGSTGGFGAYVAFVPARGIAIVMLANRNYPIEARVKAAHAIL
SQLAE
3D structure
PDB5chm Structures of FOX-4 Cephamycinase in Complex with Transition-State Analog Inhibitors.
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) S64 K67 Y150 E271 K314 S317
Catalytic site (residue number reindexed from 1) S58 K61 Y144 E265 K308 S311
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 CB4 A S64 K67 Y150 Y222 S317 G319 S58 K61 Y144 Y216 S311 G313
BS02 ZN A E124 D126 E118 D120
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:5chm, PDBe:5chm, PDBj:5chm
PDBsum5chm
PubMed32349291
UniProtQ9L387

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