Structure of PDB 4h4v Chain A

Receptor sequence
>4h4vA (length=400) Species: 358220 (Acidovorax sp. KKS102) [Search protein sequence]
LKAPVVVLGAGLASVSFVAELRQAGYQGLITVVGDEAERPYDRPPLSKDF
MAHGDAEKIRLDCKRAPEVEWLLGVTAQSFDPQAHTVALSDGRTLPYGTL
VLATGAAPRALPTLQGATMPVHTLRTLEDARRIQAGLRPQSRLLIVGGGV
IGLELAATARTAGVHVSLVCRGPRLMSRAAPATLADFVARYHAAQGVDLR
FERSVTGSVDGVVLLDDGTRIAADMVVVGIGVLANDALARAAGLACDDGI
FVDAYGRTTCPDVYALGDVTRQRNPLSGRFERIETWSNAQNQGIAVARHL
VDPTAPGYAELPWYWSDQGALRIQVAGLASGDEEIVRGEVSLDAPKFTLI
ELQKGRIVGATCVNNARDFAPLRRLLAVGAKPDRAALADPATDLRKLAAA
3D structure
PDB4h4v Random Mutagenesis with the Project Assessment for Complete Conversion of Co-Factor Specificity of a Ferredoxin Reductase BphA4
ChainA
Resolution1.4 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 1.18.1.3: ferredoxin--NAD(+) 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 I156 G272 D273 E289 T290 W291 A294 W320 G11 A13 D35 E36 R43 P44 K48 A77 T104 G105 R125 I151 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
GO:0051213 dioxygenase activity
Cellular Component
GO:0005737 cytoplasm

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Molecular Function
View graph for
Cellular Component
External links
PDB RCSB:4h4v, PDBe:4h4v, PDBj:4h4v
PDBsum4h4v
PubMed
UniProtE7FJB9

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