Structure of PDB 4e3j Chain A

Receptor sequence
>4e3jA (length=351) Species: 83333 (Escherichia coli K-12) [Search protein sequence]
APQQINDIVHRTITPLIEQQKIPGMAVAVIYQGKPYYFTWGYADIAKKQP
VTQQTLFELGSVSKTFTGVLGGDAIARGEIKLSDPTTKYWPELTAKQWNG
ITLLHLATYTAGGLPLQVPDEVKSSSDLLRFYQNWQPAWAPGTQRLYANS
SIGLFGALAVKPSGLSFEQAMQTRVFQPLKLNHTWINVPPAEEKNYAWGY
REGKAVHVSPGALDAEAYGVKSTIEDMARWVQSNLKPLDINEKTLQQGIQ
LAQSRYWQTGDMYQGLGWEMLDWPVNPDSIIALAARPVKAITPPTPAVRA
SWVHKTGATGGFGSYVAFIPEKELGIVMLANKNYPNPARVDAAWQILNAL
Q
3D structure
PDB4e3j Fragment-guided design of subnanomolar beta-lactamase inhibitors active in vivo.
ChainA
Resolution1.7999 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 Y112 A114 V121 Y150 G156 E272 K315 A318
Catalytic site (residue number reindexed from 1) S61 K64 Y109 A111 V118 Y147 G153 E269 K305 A308
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 0N4 A S64 Y150 V211 S212 Y221 A318 S61 Y147 V208 S209 Y218 A308 PDBbind-CN: -logKd/Ki=8.92,Ki=1.2nM
Gene Ontology
Molecular Function
GO:0008800 beta-lactamase activity
GO:0016787 hydrolase activity
Biological Process
GO:0017001 antibiotic catabolic process
GO:0046677 response to antibiotic
Cellular Component
GO:0030288 outer membrane-bounded periplasmic space
GO:0042597 periplasmic space

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:4e3j, PDBe:4e3j, PDBj:4e3j
PDBsum4e3j
PubMed23043117
UniProtP00811|AMPC_ECOLI Beta-lactamase (Gene Name=ampC)

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