Structure of PDB 2v34 Chain A

Receptor sequence
>2v34A (length=269) Species: 63363 (Aquifex aeolicus) [Search protein sequence]
HMIKVLSPAKINLGLWVLGRLPSGYHEILTLYQEIPFYDEIYIREGVLRV
ETNIGIPQEENLVYKGLREFERITGIEINYSIFIQKNIPPGAGLGGGSSN
LAVVLKKVNELLGSPLSEEELRELVGSISADAPFFLLGKSAIGRGKGEVL
EPVETEISGKITLVIPQVSSSTGRVYSSLREEHFVTPEYAEEKIQRIISG
EVEEIENVLGDIARELYPEINEVYRFVEYLGFKPFVSGSGSTVYFFGGAS
EELKKAAKMRGWKVVELEL
3D structure
PDB2v34 Characterization of Aquifex Aeolicus 4-Diphosphocytidyl-2C-Methyl-D-Erythritol Kinase -Ligand Recognition in a Template for Antimicrobial Drug Discovery.
ChainA
Resolution2.3 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) K9 D130
Catalytic site (residue number reindexed from 1) K10 D131
Enzyme Commision number 2.7.1.148: 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol kinase.
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 CTN A Y24 H25 K145 Y175 Y25 H26 K146 Y176
Gene Ontology
Molecular Function
GO:0005524 ATP binding
GO:0016301 kinase activity
GO:0050515 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol kinase activity
Biological Process
GO:0008299 isoprenoid biosynthetic process
GO:0016114 terpenoid biosynthetic process
GO:0016310 phosphorylation
GO:0019288 isopentenyl diphosphate biosynthetic process, methylerythritol 4-phosphate pathway

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Molecular Function
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Biological Process
External links
PDB RCSB:2v34, PDBe:2v34, PDBj:2v34
PDBsum2v34
PubMed18422643
UniProtO67060|ISPE_AQUAE 4-diphosphocytidyl-2-C-methyl-D-erythritol kinase (Gene Name=ispE)

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