Structure of PDB 2f89 Chain F Binding Site BS02

Receptor Information

>2f89 Chain F (length=346) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]

DVYAQEKQDFVQHFSQIVRVLTEDEMGHPEIGDAIARLKEVLEYNAIGGK
YNRGLTVVVAFRELVEPRKQDADSLQRAWTVGWCVELLQAFFLVADDIMD
SSLTRRGQICWYQKPGVGLDAINDANLLEACIYRLLKLYCREQPYYLNLI
ELFLQSSYQTEIGQTLDLLTAPQGNVDLVRFTEKRYKSIVKYKTAFYSFY
LPIAAAMYMAGIDGEKEHANAKKILLEMGEFFQIQDDYLDLFGDPSVTGK
IGTDIQDNKCSWLVVQCLQRATPEQYQILKENYGQKEAEKVARVKALYEE
LDLPAVFLQYEEDSYSHIMALIEQYAAPLPPAVFLGLARKIYKRRK

Ligand information

Ligand ID

InChI

InChI=1S/Mn/q+2

InChIKey

WAEMQWOKJMHJLA-UHFFFAOYSA-N

SMILES

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

Formula

Name

MANGANESE (II) ION

PDB chain

2f89 Chain F Residue 5001 [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	2f89 Structural basis for the exceptional in vivo efficacy of bisphosphonate drugs.
Resolution	2.6 Å
Binding residue (original residue number in PDB)	D103 D107
Binding residue (residue number reindexed from 1)	D96 D100
Annotation score	1

Enzymatic activity

Enzyme Commision number

2.5.1.1: dimethylallyltranstransferase.
2.5.1.10: (2E,6E)-farnesyl diphosphate synthase.

Gene Ontology

	Molecular Function
GO:0004659	prenyltransferase activity
GO:0016765	transferase activity, transferring alkyl or aryl (other than methyl) groups

	Biological Process
GO:0008299	isoprenoid biosynthetic process

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Molecular Function

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Biological Process

External links

PDB	RCSB:2f89, PDBe:2f89, PDBj:2f89
PDBsum	2f89
PubMed	16892359
UniProt	P14324\|FPPS_HUMAN Farnesyl pyrophosphate synthase (Gene Name=FDPS)

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