Structure of PDB 2bsa Chain A

Receptor sequence
>2bsaA (length=295) Species: 1167 (Anabaena sp.) [Search protein sequence]
DVPVNLYRPNAPFIGKVISNEPLVKEGGIGIVQHIKFDLTGGNLKYIEGQ
SIGIIPPGVDKNGKPEKLRLYSIASTRHGDDVDDKTISLCVRQLEYKHPE
SGATVYGVCSTYLTHIEPGSEVKITGPVGKEMLLPDDPEANVIMLATGTG
IAPMRTYLWRMFKDAERAANPEYQFKGFSWLVFGVPTTPNILYKEELEEI
QQKYPDNFRLTYAISREQKNPQGGRMYIQDRVAEHADQLWQLIKNQKTHT
YICGLRGMEEGIDAALSAAAAKEGVTWSDYQKDLKKAGRWHVETS
3D structure
PDB2bsa C-Terminal Tyrosine of Ferredoxin-Nadp(+) Reductase in Hydride Transfer Processes with Nad(P)(+)/H.
ChainA
Resolution1.92 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) Y79 S80 C261 E301 S303
Catalytic site (residue number reindexed from 1) Y71 S72 C253 E293 S295
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 R77 L78 Y79 S80 C98 L102 Y104 G115 V116 C117 S118 T157 R69 L70 Y71 S72 C90 L94 Y96 G107 V108 C109 S110 T149
BS02 NAP A S80 R100 G156 T157 P194 S223 Y235 Q237 C261 G262 L263 G265 M266 E301 T302 S303 S72 R92 G148 T149 P186 S215 Y227 Q229 C253 G254 L255 G257 M258 E293 T294 S295 MOAD: Kd<0.01uM
Gene Ontology
Molecular Function
GO:0016491 oxidoreductase activity

View graph for
Molecular Function
External links
PDB RCSB:2bsa, PDBe:2bsa, PDBj:2bsa
PDBsum2bsa
PubMed16216071
UniProtP21890|FENR_NOSSO Ferredoxin--NADP reductase (Gene Name=petH)

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