Structure of PDB 5f1g Chain A

Receptor sequence
>5f1gA (length=351) Species: 562 (Escherichia coli) [Search protein sequence]
HHPQQINDIVHRTITPLIEQQKIPGMAVAVIYQGKPYYFTWGYADIAKKQ
PVTQQTLFELGSVSKTFTGVLGGDAIARGEIKLSDPATKYWPELTAKQWN
GITLLHLATYTAGGLPLQVPDEVKSSSDLLRFYQNWQPAWAPGTQRLYAN
SSIGLFGALAVKPSGLSFEQAMQTRVFQPLKLNHTWINVPPPEEKNYAWG
YREGKAVHVSPGALDAEAYGVKSTIEDMARWVRSNMNPRDINDKTLQQGI
QLAQSRYWQTGDMYQGLGWEMLDWPVNPDSIINAAHPVKAITPPTPAVRA
SWVHKTGATGGFGSYVAFIPEKELGIVMLANKNYPNPARVAAAWQILNAL
Q
3D structure
PDB5f1g Structural and mechanistic insights into the inhibition of class C beta-lactamases through the adenylylation of the nucleophilic serine.
ChainA
Resolution1.76 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) S61 K64 Y109 A111 V118 Y147 G153 E269 K314 A317
Catalytic site (residue number reindexed from 1) S62 K65 Y110 A112 V119 Y148 G154 E270 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 AMP A S61 Q117 D120 Y147 N149 Y218 G316 A317 T318 S62 Q118 D121 Y148 N150 Y219 G307 A308 T309
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
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

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:5f1g, PDBe:5f1g, PDBj:5f1g
PDBsum5f1g
PubMed27999057
UniProtA7TUE6

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