Structure of PDB 3g30 Chain A

Receptor sequence
>3g30A (length=262) Species: 562 (Escherichia coli) [Search protein sequence]
TSAVQQKLAALEKSSGGRLGVALIDTADNTQVLYRGDERFPMCSTSKVMA
AAAVLKQSETQKQLLNQPVEIKPADLVNYNPIAEKHVNGTMTLAELSAAA
LQYSDNTAMNKLIAQLGGPGGVTAFARAIGDETFRLDRTEPTLNTAIPGD
PRDTTTPRAMAQTLRQLTLGHALGETQRAQLVTWLKGNTTGAASIRAGLP
TSWTAGDKTGSGDYGTTNDIAVIWPQGRAPLVLVTYFTQPQQNAESRRDV
LASAARIIAEGL
3D structure
PDB3g30 Molecular docking and ligand specificity in fragment-based inhibitor discovery
ChainA
Resolution1.8 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 S237
Catalytic site (residue number reindexed from 1) S44 K47 S104 E140 K208 S211
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 G30 A S70 S130 N132 N170 S237 G238 D240 S44 S104 N106 N144 S211 G212 D213 MOAD: Ki=3.1mM
PDBbind-CN: -logKd/Ki=2.51,Ki=3.1mM
BS02 G30 A T149 A150 R153 T123 A124 R127 MOAD: Ki=3.1mM
PDBbind-CN: -logKd/Ki=2.51,Ki=3.1mM
Gene Ontology
Molecular Function
GO:0008800 beta-lactamase activity
GO:0016787 hydrolase 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:3g30, PDBe:3g30, PDBj:3g30
PDBsum3g30
PubMed19305397
UniProtQ9L5C8

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