Structure of PDB 3ojg Chain A Binding Site BS02

Receptor Information

>3ojg Chain A (length=323) Species: 1462 (Geobacillus kaustophilus) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]

EMVETVCGPVPVEQLGKTLIHEHFLFGYPGFQGDVTRGTFREDESLRVAV
EAAEKMKRHGIQTVVDPTPNDCGRNPAFLRRVAEETGLNIICATGYYYEG
EGAPPYFQFRRLLGTAEDDIYDMFMAELTEGIADTGIKAGVIKLASSKGR
ITEYEKMFFRAAARAQKETGAVIITHTQEGTMGPEQAAYLLEHGADPKKI
VIGHMCGNTDPDYHRKTLAYGVYIAFDRFGIQGMVGAPTDEERVRTLLAL
LRDGYEKQIMLSHNTVNVWLGRPFTLPEPFAEMMKNWHVEHLFVNIIPAL
KNEGIRDEVLEQMFIGNPAALFS

Ligand information

Ligand ID

InChI

InChI=1S/Fe/q+3

InChIKey

VTLYFUHAOXGGBS-UHFFFAOYSA-N

SMILES

Software	SMILES
ACDLabs 10.04 CACTVS 3.341 OpenEye OEToolkits 1.5.0	[Fe+3]

Formula

Name

FE (III) ION

PDB chain

3ojg Chain A Residue 402 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]

Receptor-Ligand Complex Structure

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Structure summary

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PDB	3ojg Directed evolution of a thermostable quorum-quenching lactonase from the amidohydrolase superfamily
Resolution	1.6 Å
Binding residue (original residue number in PDB)	Y99 K145 H178 H206
Binding residue (residue number reindexed from 1)	Y97 K143 H176 H204
Annotation score	4

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.-.-

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
PDBsum	3ojg
PubMed	20980257
UniProt	Q5KZU5

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