Structure of PDB 4jzx Chain A

Receptor sequence
>4jzxA (length=362) Species: 5664 (Leishmania major) [Search protein sequence]
MAHMERFQKVYEEVQEFLLGDAEKRFEMDVHRKGYLKSMMDTTCLGGKYN
RGLCVVDVAEAMAKDTQMDAAAMERVLHDACVCGWMIEMLQAHFLVEDDI
MDHSKTRRGKPCWYLHPGVTAQVAINDGLILLAWATQMALHYFADRPFLA
EVLRVFHDVDLTTTIGQLYDVTSMVDSAKLDAKVAHANTTDYVEYTPFNH
RRIVVYKTAYYTYWLPLVMGLLVSGTLEKVDKKATHKVAMVMGEYFQVQD
DVMDCFTPPEKLGKIGTDIEDAKCSWLAVTFLTTAPAEKVAEFKANYGST
DPAAVAVIKQLYTEQNLLARFEEYEKAVVAEVEQLIAALEAQNAAFAASV
KVLWSKTYKRQK
3D structure
PDB4jzx Structural and thermodynamic basis of the inhibition of Leishmania major farnesyl diphosphate synthase by nitrogen-containing bisphosphonates.
ChainA
Resolution1.8 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) K48 H93 D98 D102 R107 D170 K207 F246 D250 D251
Catalytic site (residue number reindexed from 1) K48 H93 D98 D102 R107 D170 K207 F246 D250 D251
Enzyme Commision number 2.5.1.1: dimethylallyltranstransferase.
2.5.1.10: (2E,6E)-farnesyl diphosphate synthase.
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 IPE A G47 K48 R51 Q91 R108 T208 F246 Q247 D250 G47 K48 R51 Q91 R108 T208 F246 Q247 D250
BS02 476 A F94 D98 R107 Q167 K207 D250 K264 F94 D98 R107 Q167 K207 D250 K264 MOAD: Kd=198.6nM
BS03 CA A D98 D102 D98 D102
BS04 CA A D98 D102 D98 D102
Gene Ontology
Molecular Function
GO:0004161 dimethylallyltranstransferase activity
GO:0004337 geranyltranstransferase activity
GO:0004659 prenyltransferase activity
GO:0016740 transferase activity
GO:0016765 transferase activity, transferring alkyl or aryl (other than methyl) groups
GO:0046872 metal ion binding
Biological Process
GO:0008299 isoprenoid biosynthetic process
GO:0045337 farnesyl diphosphate 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:4jzx, PDBe:4jzx, PDBj:4jzx
PDBsum4jzx
PubMed24598749
UniProtQ4QBL1

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