Structure of PDB 3g35 Chain A

Receptor sequence
>3g35A (length=259) Species: 562 (Escherichia coli) [Search protein sequence]
AVQQKLAALEKSSGGRLGVALIDTADNTQVLYRGDERFPMCSTSKVMAAA
AVLKQSETQKQLLNQPVEIKPADLVNYNPIAEKHVNGTMTLAELSAAALQ
YSDNTAMNKLIAQLGGPGGVTAFARAIGDETFRLDRTEPTLNTAIPGDPR
DTTTPRAMAQTLRQLTLGHALGETQRAQLVTWLKGNTTGAASIRAGLPTS
WTAGDKTGSGDYGTTNDIAVIWPGRAPLVLVTYFTQPQQNAESRRDVLAS
AARIIAEGL
3D structure
PDB3g35 Molecular docking and ligand specificity in fragment-based inhibitor discovery
ChainA
Resolution1.41 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) S42 K45 S102 E138 K206 S209
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 F13 A N104 Y105 S130 N132 P167 N170 T235 G236 S237 D240 N76 Y77 S102 N104 P139 N142 T207 G208 S209 D211 MOAD: Ki=0.021mM
PDBbind-CN: -logKd/Ki=4.68,Ki=0.021mM
BS02 F13 A K82 L142 G147 A154 K54 L114 G119 A126 MOAD: Ki=0.021mM
PDBbind-CN: -logKd/Ki=4.68,Ki=0.021mM
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:3g35, PDBe:3g35, PDBj:3g35
PDBsum3g35
PubMed19305397
UniProtQ9L5C8

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