Structure of PDB 6jst Chain A

Receptor sequence
>6jstA (length=323) Species: 235909 (Geobacillus kaustophilus HTA426) [Search protein sequence]
EMVETVCGPVPVEQLGKTLIHEHFLFGYPGFQGDVTRGTFREDESLRVAV
EAAEKMKRHGIQTVVDPTPNDCGRNPAFLRRVAEETGLNIICATGYPYEG
EGAPPYFQFRRLLGTAEDDIYDMFMAELTEGIADTGIKAGVIKLASSKGR
ITEYEKMFFRAAARAQKETGAVIITHTQEGTMGPEQAAYLLEHGADPKKI
VIGHMCGNTDPDYHRKTLAYGVYIAFDRFGIQGMVGAPTDEERVRTLLAL
LRDGYEKQIMLSHNTVNVWLGRPFTLPEPFAEMMKNWHVEHLFVNIIPAL
KNEGIRDEVLEQMFIGNPAALFS
3D structure
PDB6jst Directed Computational Evolution of Quorum-Quenching Lactonases from the Amidohydrolase Superfamily.
ChainA
Resolution1.726 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 FE A H23 H25 K145 N266 H21 H23 K143 N264
BS02 ZN A K145 H178 H206 K143 H176 H204
BS03 LAE A Y30 N266 V268 F276 L278 W289 Y28 N264 V266 F274 L276 W287
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:6jst, PDBe:6jst, PDBj:6jst
PDBsum6jst
PubMed32320671
UniProtQ5KZU5

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