Structure of PDB 2gr1 Chain A

Receptor sequence
>2gr1A (length=401) Species: 307 (Pseudomonas sp. KKS102) [Search protein sequence]
LKAPVVVLGAGLASVSFVAELRQAGYQGLITVVGDEAERPYDRPPLSKDF
MAHGDAEKIRLDCKRAPEVEWLLGVTAQSFDPQAHTVALSDGRTLPYGTL
VLATGAAPRALPTLQGATMPVHTLRTLEDARRIQAGLRPQSRLLIVGGGV
IGLELAATARTAGVHVSLVETQPRLMSRAAPATLADFVARYHAAQGVDLR
FERSVTGSVDGVVLLDDGTRIAADMVVVGIGVLANDALARAAGLACDDGI
FVDAYGRTTCPDVYALGDVTRQRNPLSGRFERIETWSNAQNQGIAVARHL
VDPTAPGYAELPWYWSDQGALRIQVAGLASGDEEIVRGEVSLDAPKFTLI
ELQKGRIVGATCVNNARDFAPLRRLLAVGAKPDRAALADPATDLRKLAAA
V
3D structure
PDB2gr1 A ferredoxin reductase BphA4 uses a butterfly motion of FAD to regulate affinity for ferredoxin
ChainA
Resolution1.8 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) L17 R48 P49 Q295
Catalytic site (residue number reindexed from 1) L12 R43 P44 Q290
Enzyme Commision number 1.18.1.2: ferredoxin--NADP(+) reductase.
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 G16 A18 D40 R48 P49 A82 T109 G110 L129 R130 I156 E159 G272 D273 E289 T290 W291 A294 W320 G11 A13 D35 R43 P44 A77 T104 G105 L124 R125 I151 E154 G267 D268 E284 T285 W286 A289 W315
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0016491 oxidoreductase activity
GO:0016651 oxidoreductase activity, acting on NAD(P)H
Cellular Component
GO:0005737 cytoplasm

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Molecular Function
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Cellular Component
External links
PDB RCSB:2gr1, PDBe:2gr1, PDBj:2gr1
PDBsum2gr1
PubMed
UniProtQ52437

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