Structure of PDB 8dos Chain B

Receptor sequence
>8dosB (length=246) Species: 573 (Klebsiella pneumoniae) [Search protein sequence]
DWVSGKVTKVEYWTDALFSLYVRAPVHPFTAGQFTKLGLEIDGERVQRAY
SYVNAPGNPDLEFYLVTVPEGKLSPRLASLKPGDEVLVVSEAAGFFVLEE
VPDCDTLWMLATGTALGPYLSILQEGKDLERFNNLVLVHAVRYAADLSYL
PLMRELEQRYAGKLRIQTVVSRETVEGSLTGRVPFLIETGALEEAVGLPM
TTDTSHVMLCGNPQMVRDTQQLLKETRQMTKHLRRRPGHMTAEHYW
3D structure
PDB8dos Crystal structure of Ferredoxin (flavodoxin):NADP(+) oxidoreductase from Klebsiella pneumoniae
ChainB
Resolution1.872 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 1.18.1.2: ferredoxin--NADP(+) reductase.
1.19.1.1: flavodoxin--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 B F36 R50 A51 Y52 S53 Y66 L67 V68 V70 G73 K74 L75 S76 T116 Y247 W248 F34 R48 A49 Y50 S51 Y64 L65 V66 V68 G71 K72 L73 S74 T114 Y245 W246
BS02 NAP B V68 T114 V143 R144 D148 S173 R174 R184 N214 Q216 M217 V66 T112 V141 R142 D146 S171 R172 R182 N212 Q214 M215
Gene Ontology
Molecular Function
GO:0000104 succinate dehydrogenase activity
GO:0000166 nucleotide binding
GO:0003994 aconitate hydratase activity
GO:0004324 ferredoxin-NADP+ reductase activity
GO:0016491 oxidoreductase activity
GO:0046872 metal ion binding
Biological Process
GO:0034599 cellular response to oxidative stress
GO:0042167 heme catabolic process
Cellular Component
GO:0005737 cytoplasm

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Molecular Function

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Biological Process

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Cellular Component
External links
PDB RCSB:8dos, PDBe:8dos, PDBj:8dos
PDBsum8dos
PubMed
UniProtA0A0G3NED2

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