Structure of PDB 2iof Chain K Binding Site BS02

Receptor Information

>2iof Chain K (length=256) Species: 1396 (Bacillus cereus) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]

KIEAVIFDWAGTTVDYGCFAPLEVFMEIFHKRGVAITAEEARKPMGLLKI
DHVRALTEMPRIASEWNRVFRQLPTEADIQEMYEEFEEILFAILPRYASP
INGVKEVIASLRERGIKIGSTTGYTREMMDIVAKEAALQGYKPDFLVTPD
DVPAGRPYPWMCYKNAMELGVYPMNHMIKVGDTVSDMKEGRNAGMWTVGV
ILGSSELGLTEEEVENMDSVELREKIEVVRNRFVENGAHFTIETMQELES
VMEHIE

Ligand information

Ligand ID

InChI

InChI=1S/Mg/q+2

InChIKey

JLVVSXFLKOJNIY-UHFFFAOYSA-N

SMILES

Software	SMILES
ACDLabs 10.04 OpenEye OEToolkits 1.5.0	[Mg+2]
CACTVS 3.341	[Mg++]

Formula

Name

MAGNESIUM ION

PDB chain

2iof Chain K Residue 462 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]

Receptor-Ligand Complex Structure

Global view

Local view

Structure summary

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]

PDB	2iof Diversification of function in the haloacid dehalogenase enzyme superfamily: The role of the cap domain in hydrolytic phosphoruscarbon bond cleavage.
Resolution	2.5 Å
Binding residue (original residue number in PDB)	D12 A14 D186
Binding residue (residue number reindexed from 1)	D8 A10 D182
Annotation score	1

Enzymatic activity

Enzyme Commision number

3.11.1.1: phosphonoacetaldehyde hydrolase.

Gene Ontology

	Molecular Function
GO:0000287	magnesium ion binding
GO:0003824	catalytic activity
GO:0016787	hydrolase activity
GO:0046872	metal ion binding
GO:0050194	phosphonoacetaldehyde hydrolase activity

	Biological Process
GO:0019700	organic phosphonate catabolic process

View graph for
Molecular Function

View graph for
Biological Process

External links

PDB	RCSB:2iof, PDBe:2iof, PDBj:2iof
PDBsum	2iof
PubMed	17070898
UniProt	O31156\|PHNX_BACCE Phosphonoacetaldehyde hydrolase (Gene Name=phnX)

[Back to BioLiP]