Structure of PDB 6npc Chain A

Receptor sequence
>6npcA (length=378) Species: 506591 (Leisingera caerulea) [Search protein sequence]
HHMPRSVTADASGSFLTLTFEDGSESRFHAIWLRDNALDPETRSPGNGQR
LITIGDIPADTRISTALVDDGALTVTFAPEGKTVTFPGKWLKSNAYDTDQ
SSEVGRTSPDVETWDSSQPAPAFDWNEVQSDPKAKRDWLDAIARLGFAKL
VNGPVREGALIECASMFGFVRETNYGKYFEVRTEVNPTNLAYTGLGLQAH
TDNPYRDPVPSLQILYCLENSAEGGDSIVVDGFRAAERLRDEDPEGFALL
AGNPARFEYKGSDGVHLRARRPMIELSPDGEMIAIRFNNRSSAPFVDIPF
EKMEAYYAAYRRLGEFIDDPEMGVSFKLEPGESFIVDNTRVLHARLGYSG
SGSRWLQGCYADKDGLFSTLNVLNAQLG
3D structure
PDB6npc A New Microbial Pathway for Organophosphonate Degradation Catalyzed by Two Previously Misannotated Non-Heme-Iron Oxygenases.
ChainA
Resolution1.7 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 1.14.11.72: [2-(trimethylamino)ethyl]phosphonate dioxygenase.
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 FE2 A H198 D200 H341 H200 D202 H343
BS02 AKG A V179 L195 H198 D200 H341 R343 R352 V181 L197 H200 D202 H343 R345 R354
BS03 KVV A Y173 F177 N187 A189 Y190 D200 N201 Y203 N286 R288 Y358 Y175 F179 N189 A191 Y192 D202 N203 Y205 N288 R290 Y360
Gene Ontology
Molecular Function
GO:0005506 iron ion binding
GO:0008336 gamma-butyrobetaine dioxygenase activity
GO:0016491 oxidoreductase activity
GO:0016706 2-oxoglutarate-dependent dioxygenase activity
GO:0046872 metal ion binding
GO:0051213 dioxygenase activity
Biological Process
GO:0045329 carnitine biosynthetic process

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Molecular Function
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Biological Process
External links
PDB RCSB:6npc, PDBe:6npc, PDBj:6npc
PDBsum6npc
PubMed30789718
UniProtA0A4V8H042|TMPA_LEICA [2-(trimethylamino)ethyl]phosphonate dioxygenase (Gene Name=tmpA)

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