Structure of PDB 3da1 Chain A

Receptor sequence
>3da1A (length=496) Species: 272558 (Halalkalibacterium halodurans C-125) [Search protein sequence]
MFSAKKRDKCIGEMSEKQLDLLVIGGGITGAGIALDAQVRGIQTGLVEMN
DFASGTSSRSTKLVHGVGKERAIVYENAPHVTTPEWMLLPIFKRYMLNEK
QTLEKEPLLRKENLKGGGIYVEYRTDDARLTLEIMKEAVARGAVALNYMK
VESFIYDQGKVVGVVAKDRLTDTTHTIYAKKVVNAAGPWVDTLREKDRSK
HGKYLKLSKGVHLVVDQSRFPLRQAVYFDTESDGRMIFAIPREGKTYIGT
TDTFYDKDIASPRMTVEDRDYILAAANYMFPSLRLTADDVESSWAGLRPL
IHEDEIFFSDSGLISIAGGKLTGYRKMAERTVDAVAQGLNVNEPCTTAAI
RLSGGLAEGAQGFPRFLDEASRKGAKLGFDADEVRRLAKLYGSNVDHVLN
YAYEGKEEAEHYGLPALLLGQLQYGVEQEMVATPLDFFVRRTGALFFNIS
LVHQWKEAVLRWMAEEFSWTEEEKTRFQNELETELKMAVDPLFQVE
3D structure
PDB3da1 X-Ray structure of the glycerol-3-phosphate dehydrogenase from Bacillus halodurans complexed with FAD. Northeast Structural Genomics Consortium target BhR167.
ChainA
Resolution2.7 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 1.1.5.3: glycerol-3-phosphate dehydrogenase.
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 G27 I28 T29 E48 M49 G55 S57 S60 T61 L63 H65 V193 G229 W231 L235 G252 T292 G338 R340 G372 K373 L374 I24 G27 I28 T29 E48 M49 G55 S57 S60 T61 L63 H65 V151 G187 W189 L193 G210 T250 G296 R298 G319 K320 L321
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0004368 glycerol-3-phosphate dehydrogenase (quinone) activity
GO:0016491 oxidoreductase activity
Biological Process
GO:0006071 glycerol metabolic process
GO:0006072 glycerol-3-phosphate metabolic process
GO:0006796 phosphate-containing compound metabolic process
GO:0019563 glycerol catabolic process
GO:0019637 organophosphate metabolic process
Cellular Component
GO:0009331 glycerol-3-phosphate dehydrogenase (FAD) complex

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:3da1, PDBe:3da1, PDBj:3da1
PDBsum3da1
PubMed
UniProtQ9KDW6

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