Structure of PDB 3aqc Chain D

Receptor sequence
>3aqcD (length=325) Species: 1270 (Micrococcus luteus) [Search protein sequence]
MIALSYKAFLNPYIIEVEKRLYECIQSDSETINKAAHHILSSGGKRVRPM
FVLLSGFLNDTQKDDLIRTAVSLELVHMASLVHDDYIDNSDMRRGNTSVH
IAFDKDTAIRTGHFLLARALQNIATINNSKFHQIFSKTILEVCFGEFDQM
ADRFNYPVSFTAYLRRINRKTAILIEASCHLGALSSQLDEQSTYHIKQFG
HCIGMSYQIIDDILDYTSDEATLGKPVGSDIRNGHITYPLMAAIANLKEQ
DDDKLEAVVKHLTSTSDDEVYQYIVSQVKQYGIEPAELLSRKYGDKAKYH
LSQLQDSNIKDYLEEIHEKMLKRVY
3D structure
PDB3aqc Crystal structure of heterodimeric hexaprenyl diphosphate synthase from Micrococcus luteus B-P 26 reveals that the small subunit is directly involved in the product chain length regulation.
ChainD
Resolution2.61 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 2.5.1.83: hexaprenyl-diphosphate synthase [(2E,6E)-farnesyl-diphosphate specific].
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 MG D D84 D88 D84 D88
BS02 MG D D84 D88 D84 D88
BS03 2DE D S80 D84 R93 E146 K170 S80 D84 R93 E146 K170
Gene Ontology
Molecular Function
GO:0000287 magnesium ion binding
GO:0004659 prenyltransferase activity
GO:0016740 transferase activity
GO:0016765 transferase activity, transferring alkyl or aryl (other than methyl) groups
GO:0036423 hexaprenyl-diphosphate synthase ((2E,6E)-farnesyl-diphosphate specific) activity
GO:0046872 metal ion binding
Biological Process
GO:0008299 isoprenoid biosynthetic process
GO:0009234 menaquinone biosynthetic process

View graph for
Molecular Function

View graph for
Biological Process
External links
PDB RCSB:3aqc, PDBe:3aqc, PDBj:3aqc
PDBsum3aqc
PubMed21068379
UniProtO66129|HEXB_MICLU Hexaprenyl-diphosphate synthase large subunit ((2E,6E)-farnesyl-diphosphate specific) (Gene Name=hexs-b)

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