Structure of PDB 2gr2 Chain A

Receptor sequence

>2gr2A (length=401) Species: 307 (Pseudomonas sp. KKS102) [Search protein sequence]

LKAPVVVLGAGLASVSFVAELRQAGYQGLITVVGDEAERPYDRPPLSKDF
MAHGDAEKIRLDCKRAPEVEWLLGVTAQSFDPQAHTVALSDGRTLPYGTL
VLATGAAPRALPTLQGATMPVHTLRTLEDARRIQAGLRPQSRLLIVGGGV
IGLELAATARTAGVHVSLVETQPRLMSRAAPATLADFVARYHAAQGVDLR
FERSVTGSVDGVVLLDDGTRIAADMVVVGIGVLANDALARAAGLACDDGI
FVDAYGRTTCPDVYALGDVTRQRNPLSGRFERIETWSNAQNQGIAVARHL
VDPTAPGYAELPWYWSDQGALRIQVAGLASGDEEIVRGEVSLDAPKFTLI
ELQKGRIVGATCVNNARDFAPLRRLLAVGAKPDRAALADPATDLRKLAAA
V

3D structure

PDB

2gr2 A ferredoxin reductase BphA4 uses a butterfly motion of FAD to regulate affinity for ferredoxin

Chain

Resolution

1.85 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 E41 R48 P49 K53 A82 T109 G110 R130 G272 D273 T290 W291 A294 W320	G11 A13 D35 E36 R43 P44 K48 A77 T104 G105 R125 G267 D268 T285 W286 A289 W315
BS02	APR	A	R114 V151 G152 G154 V155 I156 E175 T176 R183 G234 I235 G236 E289	R109 V146 G147 G149 V150 I151 E170 T171 R178 G229 I230 G231 E284

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

View graph for
Molecular Function

View graph for
Cellular Component

External links

PDB	RCSB:2gr2, PDBe:2gr2, PDBj:2gr2
PDBsum	2gr2
PubMed
UniProt	Q52437

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