Structure of PDB 6pd1 Chain D

Receptor sequence
>6pd1D (length=611) Species: 243275 (Treponema denticola ATCC 35405) [Search protein sequence]
MIKQAVILAGGLGKTMPKGFLEIGGTAIVEQSVQKLLAHGIEKIVIGTGH
CNEYYDNLAKKYPAIITVKNENYANTGSMGTLEVCASFVNESFLLLESDL
IYDSAGLFSLINDERKNLILASGATKSGDEVYLEADEKNCLTGLSKNRDA
LKNIFGELVGITKLTKSTLDKMCAYAKIHHSDLPKMEYEHALLEAAKTIP
VAIKRIEYFVWREIDNEDHLEMAVKNIYPHIVENEKLRAVRREVLLNPGP
ATTTDSVKYAQVSADICPREKAFGDLMQWLCDELKLFALASETNPDEYET
VMFGCSGTGADEVMVSSCVPDTGRLLVIDNGSYGARMAKIADIYKIPMDI
FKSSTYEPLDLQKLEAEFATKKYTHLACVYHETTTGLLNPLHIICPMAKK
YGMVTIVDAVSAYCGMPMDLKSLGIDFMASTSNKNIQGMAGVGFVICNKA
ELEKTKDYPMRNYYLNLYDQYAYFAKTHQTRFTPPVQTMYALRQAVLETK
QETVQKRYERYTACWNILVAAIKKLGLKMLVKEEHQSHFITAILEPETPK
YSFEALHDFAAEHSFTIYPGKLGNIDTFRIANIGDIQPEEMRRFTVKLKE
YMNGIGVGVLE
3D structure
PDB6pd1 The predominance of nucleotidyl activation in bacterial phosphonate biosynthesis.
ChainD
Resolution2.72 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 2.6.1.37: 2-aminoethylphosphonate--pyruvate transaminase.
2.7.7.107: (2-aminoethyl)phosphonate cytidylyltransferase.
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 E104 D106 E97 D99
Gene Ontology
Molecular Function
GO:0008483 transaminase activity
GO:0016779 nucleotidyltransferase activity
GO:0046872 metal ion binding
GO:0047304 2-aminoethylphosphonate-pyruvate transaminase activity
Biological Process
GO:0019700 organic phosphonate catabolic process
GO:0032923 organic phosphonate biosynthetic process

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:6pd1, PDBe:6pd1, PDBj:6pd1
PDBsum6pd1
PubMed31420548
UniProtQ73MU2|PNTCW_TREDE Bifunctional 2-aminoethylphosphonate cytidylyltransferase/aminotransferase (Gene Name=pntC)

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