Structure of PDB 5f1f Chain A

Receptor sequence
>5f1fA (length=361) Species: 548 (Klebsiella aerogenes) [Search protein sequence]
HHGEASPVDPLRPVVDASIQPLLKEHRIPGMAVAVLKDGKAHYFNYGVAN
RESGAGVSEQTLFEIGSVSKTLTATLGAYAVVKGAMQLDDKASRHAPWLK
GSAFDSITMGELATYSAGGLPLQFPEEVDSSEKMRAYYRQWAPVYSPGSH
RQYSNPSIGLFGHLAASSLKQPFAPLMEQTLLPGLGMHHTYVNVPKQAMA
SYAYGYSKEDKPIRVNPGMLADEAYGIKTSSADLLRFVKANIGGVDDKAL
QQAISLTHQGHYSVGGMTQGLGWESYAYPVTEQTLLAGNSAKVILEANPT
AAPRESGSQVLFNKTGSTNGFGAYVAFVPARGIGIVMLANRNYPIEARIK
AAHAILAQLAG
3D structure
PDB5f1f Structural and mechanistic insights into the inhibition of class C beta-lactamases through the adenylylation of the nucleophilic serine.
ChainA
Resolution1.548 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) S65 K68 M107 E109 F122 Y151 G157 E272 K312 S315
Catalytic site (residue number reindexed from 1) S67 K70 M109 E111 F124 Y153 G159 E274 K314 S317
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 S65 Q121 Y151 Y223 G314 S315 T316 S67 Q123 Y153 Y225 G316 S317 T318
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
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

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:5f1f, PDBe:5f1f, PDBj:5f1f
PDBsum5f1f
PubMed27999057
UniProtQ99QC1

[Back to BioLiP]