Structure of PDB 3ojg Chain A

Receptor sequence
>3ojgA (length=323) Species: 1462 (Geobacillus kaustophilus) [Search protein sequence]
EMVETVCGPVPVEQLGKTLIHEHFLFGYPGFQGDVTRGTFREDESLRVAV
EAAEKMKRHGIQTVVDPTPNDCGRNPAFLRRVAEETGLNIICATGYYYEG
EGAPPYFQFRRLLGTAEDDIYDMFMAELTEGIADTGIKAGVIKLASSKGR
ITEYEKMFFRAAARAQKETGAVIITHTQEGTMGPEQAAYLLEHGADPKKI
VIGHMCGNTDPDYHRKTLAYGVYIAFDRFGIQGMVGAPTDEERVRTLLAL
LRDGYEKQIMLSHNTVNVWLGRPFTLPEPFAEMMKNWHVEHLFVNIIPAL
KNEGIRDEVLEQMFIGNPAALFS
3D structure
PDB3ojg Directed evolution of a thermostable quorum-quenching lactonase from the amidohydrolase superfamily
ChainA
Resolution1.6 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H23 H25 K145 H178 H206 G209 R230 N266
Catalytic site (residue number reindexed from 1) H21 H23 K143 H176 H204 G207 R228 N264
Enzyme Commision number 3.5.-.-
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 ZN A H23 H25 K145 N266 H21 H23 K143 N264
BS02 FE A Y99 K145 H178 H206 Y97 K143 H176 H204
BS03 HL4 A F28 Y30 R230 M236 N266 V268 W271 F26 Y28 R228 M234 N264 V266 W269
Gene Ontology
Molecular Function
GO:0008270 zinc ion binding
GO:0016787 hydrolase activity
GO:0046872 metal ion binding
Biological Process
GO:0009056 catabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:3ojg, PDBe:3ojg, PDBj:3ojg
PDBsum3ojg
PubMed20980257
UniProtQ5KZU5

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