Structure of PDB 4h4p Chain A

Receptor sequence
>4h4pA (length=401) Species: 358220 (Acidovorax sp. KKS102) [Search protein sequence]
ALKAPVVVLGAGLASVSFVAELRQAGYQGLITVVGDEAERPYDRPPLSKD
FMAHGDAEKIRLDCKRAPEVEWLLGVTAQSFDPQAHTVALSDGRTLPYGT
LVLATGAAPRALPTLQGATMPVHTLRTLEDARRIQAGLRPQSRLLIVGGG
VIGLELAATARTAGVHVSLVQTKPRLMSRAAPATLADFVARYHAAQGVDL
RFERSVTGSVDGVVLLDDGTRIAADMVVVGIGVLANDALARAAGLACDDG
IFVDAYGRTTCPDVYALGDVTRQRNPLSGRFERIETWSNAQNQGIAVARH
LVDPTAPGYAELPWYWSDQGALRIQVAGLASGDEEIVRGEVSLDAPKFTL
IELQKGRIVGATCVNNARDFAPLRRLLAVGAKPDRAALADPATDLRKLAA
A
3D structure
PDB4h4p Random Mutagenesis with the Project Assessment for Complete Conversion of Co-Factor Specificity of a Ferredoxin Reductase BphA4
ChainA
Resolution1.502 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) L13 R44 P45 Q291
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 G12 A14 D36 E37 R44 P45 K49 A78 T105 G106 R126 I152 G268 D269 E285 T286 W287 A290 W316
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:4h4p, PDBe:4h4p, PDBj:4h4p
PDBsum4h4p
PubMed
UniProtE7FJB9

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