Structure of PDB 2rgh Chain A

Receptor sequence
>2rghA (length=546) Species: 1306 (Streptococcus sp.) [Search protein sequence]
CMFSNKTRQDSIQKMQQEELDLLIIGGGITGAGVAVQAAASGIKTGLIEM
QDFAEGTSSRSTKLVHGGIRYLKTFDVEVVADTVGERAVVQGIAPHIPKP
DPMLLPIYEDEGATTFNMFSVKVAMDLYDKLANVTGTKYENYTLTPEEVL
EREPFLKKEGLKGAGVYLDFRNNDARLVIDNIKKAAEDGAYLVSKMKAVG
FLYEGDQIVGVKARDLLTDEVIEIKAKLVINTSGPWVDKVRNLNFTRPVS
PKMRPTKGIHLVVDAKKLPVPQPTYFDTGKQDGRMVFAIPRENKTYFGTT
DTDYQGDFTDPKVTQEDVDYLLDVINHRYPEANITLADIEASWAGLRPLL
IGSSLEREPDGLLTLSGGKITDYRKMAEGALRLIRQLLKEEYGIETKEID
SKKYQISGGNFDPTKLEETVTELAKEGVAAGLEEEDATYIADFYGTNARR
IFELAKEMAPYPGLSLAESARLRYGLEEEMVLAPGDYLIRRTNHLLFERD
QLDEIKQPVIDAIAEYFGWTEEEKAQQTKRLEALIAESDLRELKGE
3D structure
PDB2rgh Structure of alpha-glycerophosphate oxidase from Streptococcus sp.: a template for the mitochondrial alpha-glycerophosphate dehydrogenase.
ChainA
Resolution2.3 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 1.1.3.21: glycerol-3-phosphate oxidase.
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 FAD A I24 G25 G27 I28 T29 E48 M49 Q50 G55 T56 S57 S60 T61 L63 K196 A197 S232 G233 W235 G257 G344 L345 R346 K429 I430 T431 I25 G26 G28 I29 T30 E49 M50 Q51 G56 T57 S58 S61 T62 L64 K197 A198 S233 G234 W236 G258 G345 L346 R347 K369 I370 T371
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0004368 glycerol-3-phosphate dehydrogenase (quinone) activity
GO:0004369 glycerol-3-phosphate oxidase activity
Biological Process
GO:0006071 glycerol metabolic process
GO:0006072 glycerol-3-phosphate metabolic process
GO:0006796 phosphate-containing compound metabolic process
GO:0019637 organophosphate metabolic process
Cellular Component
GO:0016020 membrane

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:2rgh, PDBe:2rgh, PDBj:2rgh
PDBsum2rgh
PubMed18154320
UniProtD0VWY7

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