Structure of PDB 4kkm Chain B Binding Site BS01
Receptor Information
>4kkm Chain B (length=280) Species:
264203
(Zymomonas mobilis subsp. mobilis ZM4 = ATCC 31821) [
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MAVNLKTMMEQVAQDIDRLFAEQLPVPEDPRRRLVEAMRYAAIGGGKRLR
PLLVVATCALFNVDREAALRVGMAIECIHVYSLIHDDMPCMDNDDLRRGK
PTVHKAFDDASAVLSGDALQALAFEILSEEKIHTDPHVRLELIQALAIAS
GKDGMVGGQAIDLAAETSTVPFDLPTITRLQQLKTGALFGFCLEAGAIMG
RQNKDIRDRLKAYARDIGLAFQIADDLIDAEGDGKATFLSLLGLEKARSQ
AQALVDQAIAHLSVFGSEADYLRSIARYIV
Ligand information
Ligand ID
CA
InChI
InChI=1S/Ca/q+2
InChIKey
BHPQYMZQTOCNFJ-UHFFFAOYSA-N
SMILES
Software
SMILES
CACTVS 3.341
[Ca++]
ACDLabs 10.04
OpenEye OEToolkits 1.5.0
[Ca+2]
Formula
Ca
Name
CALCIUM ION
ChEMBL
DrugBank
DB14577
ZINC
PDB chain
4kkm Chain B Residue 302 [
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Receptor-Ligand Complex Structure
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PDB
4kkm
Crystal structure of a FPP/GFPP synthase (Target EFI-501952) from Zymomonas mobilis, apo structure
Resolution
1.9 Å
Binding residue
(original residue number in PDB)
D86 D92
Binding residue
(residue number reindexed from 1)
D86 D92
Annotation score
1
Enzymatic activity
Catalytic site (original residue number in PDB)
K47 Y81 D86 D92 R97 D162 K184 F221 D225 D226
Catalytic site (residue number reindexed from 1)
K47 Y81 D86 D92 R97 D162 K184 F221 D225 D226
Enzyme Commision number
2.5.1.10
: (2E,6E)-farnesyl diphosphate synthase.
Gene Ontology
Molecular Function
GO:0004659
prenyltransferase activity
GO:0016740
transferase activity
GO:0046872
metal ion binding
Biological Process
GO:0008299
isoprenoid biosynthetic process
Cellular Component
GO:0005737
cytoplasm
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Molecular Function
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Biological Process
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Cellular Component
External links
PDB
RCSB:4kkm
,
PDBe:4kkm
,
PDBj:4kkm
PDBsum
4kkm
PubMed
UniProt
Q5NP81
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