Structure of PDB 6afp Chain A

Receptor sequence
>6afpA (length=268) Species: 57975 (Burkholderia thailandensis) [Search protein sequence]
GSHMRNVAAEQQLRELESTFDGRLGFVALDTATGARIAHRADERFPFCST
FKTMLSAAVLARSAGDAALLQRRIPYAKRDLVRYSPITEKHVGAGMTVAE
LCAATLQYSDNTAADLLIALLGGPQAVTAYARSIGDATFRLDRRETELNT
AIPGDERDTTTPAAMAASVRRLLVGDALGTAQRAQLNAWMLGNKTGDARI
RAGVPAGWRVADKTGTGDYGTGNDIGVAYPPDRAPIVFVVYTTMRSRNAQ
ARDDVIASAARIAARAFV
3D structure
PDB6afp Non-catalytic-Region Mutations Conferring Transition of Class A beta-Lactamases Into ESBLs.
ChainA
Resolution1.398 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) S70 K73 S130 E166 K234 T237
Catalytic site (residue number reindexed from 1) S49 K52 S109 E145 K213 T216
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 C69 S70 K73 Y105 N132 E166 N170 T237 G238 D240 C48 S49 K52 Y84 N111 E145 N149 T216 G217 D218
Gene Ontology
Molecular Function
GO:0008800 beta-lactamase activity
Biological Process
GO:0017001 antibiotic catabolic process
GO:0030655 beta-lactam antibiotic catabolic process
GO:0046677 response to antibiotic

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Molecular Function
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Biological Process
External links
PDB RCSB:6afp, PDBe:6afp, PDBj:6afp
PDBsum6afp
PubMed
UniProtQ2T5A3

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